|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
3-472 |
0e+00 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 951.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 3 QEVILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMENNTWHQWSLDAILQRFADCCRQINSELTDCHIRGIAVTTF 82
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARASTPNASDIAAENSDWHQWSLDAILQRFADCCRQINSELTECHIRGITVTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISS 162
Cdd:PRK10331 81 GVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLFISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 163 LINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHD 242
Cdd:PRK10331 161 LINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISAGHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 243 TQFALFGAGAEQNEPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQAGLYNPGMQWLASGVLEWVRKLFWTAETPW 322
Cdd:PRK10331 241 TQFALFGSGAGQNQPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQSGLYNPGMQWLASGVLEWVRKLFWTAETPY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 323 QILIEEARLIAPGADGVKMQCDLLSCQNAGWQGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGS 402
Cdd:PRK10331 321 QTMIEEARAIPPGADGVKMQCDLLACQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGS 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 403 RNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQYRYFYPQTEPEFIEEV 472
Cdd:PRK10331 401 RNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYPQTEPEFIEEV 470
|
|
| fuculo_kin_coli |
TIGR02628 |
L-fuculokinase; Members of this family are L-fuculokinase, from the clade that includes the ... |
4-463 |
0e+00 |
|
L-fuculokinase; Members of this family are L-fuculokinase, from the clade that includes the L-fuculokinase of Escherichia coli. This enzyme catalyzes the second step in fucose catabolism. This family belongs to FGGY family of carbohydrate kinases (pfam02782, pfam00370). It is encoded by the kinase (K) gene of the fucose (fuc) operon. [Energy metabolism, Sugars]
Pssm-ID: 131676 [Multi-domain] Cd Length: 465 Bit Score: 831.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 4 EVILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMENNTWHQWSLDAILQRFADCCRQINSELTDCHIRGIAVTTFG 83
Cdd:TIGR02628 1 EVILVLDCGATNLRAIAINRQGKIVASASTPNATKQAIENNDYHIWDLEAIWQKLADCCQQINSELTEKHIRGIAVTTFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 84 VDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISSL 163
Cdd:TIGR02628 81 VDGAPFDKQGNQLYPIISWKCPRTAPVMDNIERLLDAQRLYAINGIGAYSFNTLYKLVWLKEHHPQLFERMHKFVFISSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 164 INHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHDT 243
Cdd:TIGR02628 161 ITHRLTGEFTTDITMAGTSMMTDLTQRNWSPQILQALGLSRRLFPPLVEAGEQIGTLQNSAAAMLGLPVGVPVISAGHDT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 244 QFALFGAGAEQNEPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQAGLYNPGMQWLASGVLEWVRKLFWTAETP-- 321
Cdd:TIGR02628 241 QFALFGSGAEQNQPVLSSGTWEILMARSQQVDTSLLSQYAGSTCELDSQAGLYNPAMQWLASGVLEWVRKLFFTAETPsd 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 322 --WQILIEEARLIAPGADGVK-MQCDLLSCQNAGWQGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLV 398
Cdd:TIGR02628 321 hyYQMMIEEARLIANGADGVVnFQCDLLSCGQGGIQGLTLNTTRGHIYRAALEGLTAQLKRNLQMLEQIGQFKASELLLV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446731104 399 GGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQYRYFYPQ 463
Cdd:TIGR02628 401 GGGSKNTLWNQIRANMLDIPVKVVDDAETTVAGAAMFGFYGVGEYNSPEEAQAQMHPQYRYFYPQ 465
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-441 |
8.96e-149 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 431.63 E-value: 8.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNASDiaMENNTWHQWSLDAILQRFADCCRQINSELTDCHIRGIAVTTFGV 84
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLI--HPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 85 DGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISSLI 164
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 165 NHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHDTQ 244
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 245 FALFGAGA-EQNEPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQAGLYNPGMQWLASGVLEWVRKLFWTAETPWQ 323
Cdd:cd07773 239 CAALGAGViEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLSYGHHVPGGYYYLAGSLPGGALLEWFRDLFGGDESDLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 324 ILIEEARLIAPGADGVKMQCDLLSCQN--------AGWQGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGhFKASEL 395
Cdd:cd07773 319 AADELAEAAPPGPTGLLFLPHLSGSGTpdfdpdarGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAG-IPIDEI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446731104 396 LLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVG 441
Cdd:cd07773 398 RAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
5-249 |
6.24e-113 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 332.76 E-value: 6.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMEnnTWHQWSLDAILQRFADCCRQINSEL--TDCHIRGIAVTTF 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHP--GWAEQDPDEIWQAVAQCIAKTLSQLgiSLKQIKGIGISNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISS 162
Cdd:pfam00370 79 GHGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 163 LINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHD 242
Cdd:pfam00370 159 YLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGD 238
|
....*..
gi 446731104 243 TQFALFG 249
Cdd:pfam00370 239 QQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
4-459 |
1.79e-112 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 340.66 E-value: 1.79e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 4 EVILVLDCGATNVRAIAVNRQGKIVARASTPNasDIAMENNTWHQWSLDAILQRFADCCRQINSELTDC--HIRGIAVTT 81
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEY--PLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDpeEIAAIGVSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 82 FGVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFIS 161
Cdd:COG1070 79 QMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 162 SLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGH 241
Cdd:COG1070 159 DYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 242 DTQFALFGAGA-EQNEPVLSSGTWEILMVRSAQVDTSLLSQYAGSTcelDSQAGLYNPGMQWLASG-VLEWVRKLFWTAE 319
Cdd:COG1070 239 DNAAAALGAGAvEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFC---HAVPGRWLPMGATNNGGsALRWFRDLFADGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 320 -TPWQILIEEARLIAPGADGVKMQCDL------LSCQNA--GWQGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHf 390
Cdd:COG1070 316 lDDYEELNALAAEVPPGADGLLFLPYLsgertpHWDPNArgAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGV- 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 391 KASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEA-RAQIHYQYRY 459
Cdd:COG1070 395 KIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAaAAMVRVGETI 464
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
5-436 |
3.68e-105 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 318.36 E-value: 3.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNasDIAMENNTWHQWSLDAILQRFADCCRQINSELTD--CHIRGIAVTTF 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREY--PLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIdpSDIAAIGISGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVDGALVDKQGNLLYPIISWkcprtaavMDnierlistqqlqaisgvgafsfntlyklvwlkenhpqlleRAHAWLFISS 162
Cdd:cd00366 79 MPGVVLVDADGNPLRPAIIW--------LD----------------------------------------RRAKFLQPND 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 163 LINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHD 242
Cdd:cd00366 111 YIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 243 TQFALFGAGA-EQNEPVLSSGTWEILMVRSAQ---VDTSLLSQYAGstceldsQAGLYNP-GMQWLASGVLEWVRKLFWT 317
Cdd:cd00366 191 TAAAALGAGVvEPGDAVDSTGTSSVLSVCTDEpvpPDPRLLNRCHV-------VPGLWLLeGAINTGGASLRWFRDEFGE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 318 AETPW---QILIEEARLIAPGADGV--------KMQCDLLSCQNAGWQGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEK 386
Cdd:cd00366 264 EEDSDaeyEGLDELAAEVPPGSDGLiflpylsgERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEE 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446731104 387 IGHfKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFG 436
Cdd:cd00366 344 LGV-KIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-465 |
6.32e-92 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 285.57 E-value: 6.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARAS------TPNASDIAMENNTWHQWSLDAIlqrfADCCRQINSELTDchIRGIA 78
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYreyppyYPEPGWVEQDPDDWWDALCEAL----KEAVAKAGVDPED--IAAIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 79 VTTFGVDGALVDKQGNLLYPIISWkcprtaavMDNierlistqqlqaisgvgafsfntlyklvwlkenhpqlleRAHAWL 158
Cdd:cd07779 75 LTSQRSTFVPVDEDGRPLRPAISW--------QDK---------------------------------------RTAKFL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 159 FISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVIS 238
Cdd:cd07779 108 TVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 239 AGHDTQFALFGAGA-EQNEPVLSSGTWEILMVRSAQVDTSLLSQYagsTCELDSQAGLYNP-GMQWLASGVLEWVRKLF- 315
Cdd:cd07779 188 GGGDQQCAALGAGVlEPGTASLSLGTAAVVIAVSDKPVEDPERRI---PCNPSAVPGKWVLeGSINTGGSAVRWFRDEFg 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 316 -------WTAETPWQILIEEARLIAPGADGVKMQCDLLSCQNAGWQ--------GVTLNTTRGHFYRAALEGLTTQLQRN 380
Cdd:cd07779 265 qdevaekELGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNpeargafiGLTLSHTRAHLARAILEGIAFELRDN 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 381 LQMLEKIGHfKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQYRYF 460
Cdd:cd07779 345 LEAMEKAGV-PIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTF 423
|
....*
gi 446731104 461 YPQTE 465
Cdd:cd07779 424 EPDPE 428
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
5-465 |
1.93e-85 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 270.56 E-value: 1.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARAS--------TPNASDIAMEnntwhQWsLDAILQRFADCCRQINSELTDchIRG 76
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASaeyptsspKPGWAEQDPE-----DW-WQATKEALRELLAKAGISPSD--IAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 77 IAVTtfgvdGA-----LVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFnTLYKLVWLKENHPQLL 151
Cdd:cd07808 73 IGLT-----GQmhglvLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILIITGNPPLPGF-TLPKLLWLKENEPEIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 152 ERAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLP 231
Cdd:cd07808 147 ARIRKILLPKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 232 VGIPVISAGHDTQFALFGAGA-EQNEPVLSSGTweilmvrSAQVDTSLlsqyagSTCELDSQAGLYN-----PGmQWLAS 305
Cdd:cd07808 227 EGTPVVAGAGDNAAAALGAGVvEPGDALISLGT-------SGVVFAPT------DKPVPDPKGRLHTfphavPG-KWYAM 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 306 GV-------LEWVRKLFWTAETPWQILIEEARLIAPGADGV------------KMQCDLlscqNAGWQGVTLNTTRGHFY 366
Cdd:cd07808 293 GVtlsaglsLRWLRDLFGPDRESFDELDAEAAKVPPGSEGLlflpylsgertpYWDPNA----RGSFFGLSLSHTRAHLA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 367 RAALEGLTTQLQRNLQMLEKIGhFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSP 446
Cdd:cd07808 369 RAVLEGVAFSLRDSLEVLKELG-IKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDL 447
|
490
....*....|....*....
gi 446731104 447 EEARAQIHYQYRYFYPQTE 465
Cdd:cd07808 448 EEAAAACIKIEKTIEPDPE 466
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
7-451 |
2.70e-83 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 264.39 E-value: 2.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 7 LVLDCGATNVRAIAVNRQGK-----IVARASTPnasdIAMENNTWHqWSLDAILQRFADCCRQINSELTDchIRGIAVTT 81
Cdd:cd07771 3 LAVDLGASSGRVILGSLDGGkleleEIHRFPNR----PVEINGHLY-WDIDRLFDEIKEGLKKAAEQGGD--IDSIGIDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 82 FGVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFIS 161
Cdd:cd07771 76 WGVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 162 SLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPvGIPVIS-AG 240
Cdd:cd07771 156 DLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLK-GIPVIAvAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 241 HDTQFALFGAGAEQNEPV-LSSGTWEILMVRSAQVDTSLLSQYAGSTCELdsQAG-----LYN-PGMqWLASGVL-EWVR 312
Cdd:cd07771 235 HDTASAVAAVPAEDEDAAfISSGTWSLIGVELDEPVITEEAFEAGFTNEG--GADgtirlLKNiTGL-WLLQECRrEWEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 313 KlfwTAETPWQILIEEA---------------RLIAPGADGVKMQcdlLSCQNagwQGVTLNTTRGHFYRAALEGLTTQL 377
Cdd:cd07771 312 E---GKDYSYDELVALAeeappfgafidpddpRFLNPGDMPEAIR---AYCRE---TGQPVPESPGEIARCIYESLALKY 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446731104 378 QRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVkVLDDAETTVAGAALFGWYGVGEFNSPEEARA 451
Cdd:cd07771 383 AKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPV-IAGPVEATAIGNLLVQLIALGEIKSLEEGRE 455
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
5-465 |
2.00e-82 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 262.84 E-value: 2.00e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNASDiaMENNTWHQWSLDAILQRFADCCRQI--NSELTDCHIRGIAVTTF 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTY--YPKPGWAEQDPEDWWDAVCRATRALleKSGIDPSDIAAIAFSGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFS-FNTLYKLVWLKENHPQLLERAHAWLFIS 161
Cdd:cd07805 79 MQGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSgKDPLAKILWLKENEPEIYAKTHKFLDAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 162 SLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGH 241
Cdd:cd07805 159 DYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 242 DTQFALFGAGA-EQNEPVLSSGT--WeilMVRSAQVDTSLLSQYAGSTCELDSqaGLYNP-GMQWLASGVLEWVRKLFWT 317
Cdd:cd07805 239 DAAAAALGAGAvEEGDAHIYLGTsgW---VAAHVPKPKTDPDHGIFTLASADP--GRYLLaAEQETAGGALEWARDNLGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 318 AET----PWQILIEEARLIAPGADGvkmqcdLL--------------SCQNAGWQGVTLNTTRGHFYRAALEGLTTQLQR 379
Cdd:cd07805 314 DEDlgadDYELLDELAAEAPPGSNG------LLflpwlngerspvedPNARGAFIGLSLEHTRADLARAVLEGVAFNLRW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 380 NLQMLEKIGHfKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDA-ETTVAGAALFGWYGVGEFNSPEEARAQIHYQYR 458
Cdd:cd07805 388 LLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRPVEVPENPqEAGALGAALLAAVGLGLLKSFDEAKALVKVEKV 466
|
....*..
gi 446731104 459 YfYPQTE 465
Cdd:cd07805 467 F-EPDPE 472
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-450 |
1.44e-78 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 252.48 E-value: 1.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARAStpNASDIAMENNTWHQWSLDAILQRFADCCRQINSELTDCHIRGIAVTTF-- 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSS--AEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAmh 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVdgALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISS 162
Cdd:cd07770 79 SL--LGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 163 LINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHD 242
Cdd:cd07770 157 YLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 243 TQFALFGAGA-EQNEPVLSSGTweilmvrSAQVDTSLlsqyagSTCELDSQAGL---YNPGMQWLASG-------VLEWV 311
Cdd:cd07770 237 GALANLGSGAlDPGRAALTVGT-------SGAIRVVS------DRPVLDPPGRLwcyRLDENRWLVGGainnggnVLDWL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 312 RKLFWTAETPWQILIEEARLIAPGADGVKMQCDLLSCQNAGW--------QGVTLNTTRGHFYRAALEGLTTQLQRNLQM 383
Cdd:cd07770 304 RDTLLLSGDDYEELDKLAEAVPPGSHGLIFLPYLAGERAPGWnpdargafFGLTLNHTRADILRAVLEGVAFNLKSIYEA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446731104 384 LEKIGHfKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEAR 450
Cdd:cd07770 384 LEELAG-PVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADE 449
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-441 |
2.63e-72 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 235.14 E-value: 2.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNASdIAMENNtWHQWSLDAILQRFADCCRQI--NSELTDCHIRGIAVTTF 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPV-ISPRPG-WAERDMDELWQATAEAIRELleKSGVDPSDIAGVGVTGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GvDGA-LVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFIS 161
Cdd:cd07802 79 G-NGLyLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 162 SLINHRLTGEFTTDITMAGTSqMLDIQQRDFSPQILQATGIP--RRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISA 239
Cdd:cd07802 158 DWIRYRLTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 240 GHDTQFALFGAGAeQNEPVLSS--GTWEILMVRSAQVDTSllsqYAGSTCEldsqagLYNPGMQWL-------ASGVLEW 310
Cdd:cd07802 237 AFDVVASALGAGA-VDEGQLCVilGTWSINEVVTDEPVVP----DSVGSNS------LHADPGLYLiveasptSASNLDW 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 311 VRKLFWTAE-----TPWQILIEEARLIAPGADGVKMQcDLLSCQN------AGWQGVTLNTTRGHFYRAALEGLTTQLQR 379
Cdd:cd07802 306 FLDTLLGEEkeaggSDYDELDELIAAVPPGSSGVIFL-PYLYGSGanpnarGGFFGLTAWHTRAHLLRAVYEGIAFSHRD 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446731104 380 NLQMLEKigHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVG 441
Cdd:cd07802 385 HLERLLV--ARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
6-441 |
1.58e-70 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 230.88 E-value: 1.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARASTPNasDIAMENNTW-HQWSlDAILQRFADCCRQI--NSELTDCHIRGIAVTTF 82
Cdd:cd07804 2 LLGIDIGTTGTKGVLVDEDGKVLASASIEH--DLLTPKPGWaEHDP-EVWWGAVCEIIRELlaKAGISPKEIAAIGVSGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISS 162
Cdd:cd07804 79 VPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 163 LINHRLTGEFTTDITMAG-TSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGH 241
Cdd:cd07804 159 YIVYKLTGEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 242 DTQFALFGAGA-EQNEPVL---SSGTWeILMVRSAQVDTSLLSQYagstcelDSQAGLYNPGMQWLASG-VLEWVRKLFW 316
Cdd:cd07804 239 DAAASALSAGVvEPGDLLLmlgTAGDI-GVVTDKLPTDPRLWLDY-------HDIPGTYVLNGGMATSGsLLRWFRDEFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 317 TAE---------TPWQILIEEARLIAPGADGVKM----------QCDllscQNA--GWQGVTLNTTRGHFYRAALEGLTT 375
Cdd:cd07804 311 GEEveaeksggdSAYDLLDEEAEKIPPGSDGLIVlpyfmgertpIWD----PDArgVIFGLTLSHTRAHLYRALLEGVAY 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446731104 376 QLQRNLQMLEKIGHFKAsELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVG 441
Cdd:cd07804 387 GLRHHLEVIREAGLPIK-RLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
7-441 |
2.61e-70 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 230.19 E-value: 2.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 7 LVLDCGATNVRAIAVNRQGKIVARASTPN------ASDIAMEnntwhqWSLDAILQRFADCCRQI--NSELTDCHIRGIA 78
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWeyytddDYPDAKE------FDPEELWEKICEAIREAlkKAGISPEDISAVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 79 VTTFGVDGALVDKQGNLLYpiiswKCP----RTAAVMDNIERLIsTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERA 154
Cdd:cd07798 77 STSQREGIVFLDKDGRELY-----AGPnidaRGVEEAAEIDDEF-GEEIYTTTGHWPTELFPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 155 HAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGI 234
Cdd:cd07798 151 ATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 235 PVISAGHDTQFALFGAGA-EQNEPVLSSGTWE-ILMVrsaqVDTSLLSQYAGSTCELDSQAGLY----NPGMqwlASGVL 308
Cdd:cd07798 231 PVVVGGADTQCALLGSGAiEPGDIGIVAGTTTpVQMV----TDEPIIDPERRLWTGCHLVPGKWvlesNAGV---TGLNY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 309 EWVRKLF-WTAETPWQILIEEARLIAPGADGV-------KMQCDLLSCQNAGWQ----GVTLNTTRGHFYRAALEGLTTQ 376
Cdd:cd07798 304 QWLKELLyGDPEDSYEVLEEEASEIPPGANGVlaflgpqIFDARLSGLKNGGFLfptpLSASELTRGDFARAILENIAFA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446731104 377 LQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVG 441
Cdd:cd07798 384 IRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
5-440 |
8.44e-65 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 215.16 E-value: 8.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMENntWHQWSLDAILQRFADCCRQINSELTDCHIRGIAVT---- 80
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPG--WVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDgtsg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 81 TFgvdgALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSfnTLYKLVWLKENHPQLLERAHAWLFI 160
Cdd:cd07783 79 TL----VLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSS--SLAKLLWLKRHEPEVLAKTAKFLHQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 161 SSLINHRLTG-EFTTDITMAGTSqMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISA 239
Cdd:cd07783 153 ADWLAGRLTGdRGVTDYNNALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 240 GHDTQFALFGAGA-EQNEPVLSSGTWEILMvrsaqvdtsLLSqyagSTCELDSQAGLYN---PGMQWLASGVL----EWV 311
Cdd:cd07783 232 TTDSIAAFLASGAvRPGDAVTSLGTTLVLK---------LLS----DKRVPDPGGGVYShrhGDGYWLVGGASntggAVL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 312 RKLFWTAEtpWQILIEEARliAPGADGvkmqcdLLSC-----------QNAGWQGVTL--NTTRGHFYRAALEGLTTQLQ 378
Cdd:cd07783 299 RWFFSDDE--LAELSAQAD--PPGPSG------LIYYplplrgerfpfWDPDARGFLLprPHDRAEFLRALLEGIAFIER 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446731104 379 RNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVaGAALFGWYGV 440
Cdd:cd07783 369 LGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAAL-GAALLAAAGL 429
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
9-462 |
9.74e-65 |
|
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]
Pssm-ID: 273550 [Multi-domain] Cd Length: 481 Bit Score: 216.41 E-value: 9.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 9 LDCGATNVRAIAVNRQGKIVARASTPNasDIAMENNTW-----HQWsLDAILQRFADCcrqinseLTDCHIRGIAVTTFG 83
Cdd:TIGR01312 3 IDLGTSGVKALLVDEQGEVIASGSAPH--TVISPHPGWseqdpEDW-WDATEEAIKEL-------LEQASEMGQDIKGIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 84 VDG-----ALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWL 158
Cdd:TIGR01312 73 ISGqmhglVLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 159 FISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVIS 238
Cdd:TIGR01312 153 LPKDYLRYRLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 239 AGHDTQFALFGAGA-EQNEPVLSSGTWEIL--MVRSAQVD-TSLLSQYAGSTceldsqaglynPGmQWLASGV------- 307
Cdd:TIGR01312 233 GGGDNAAGAIGTGTvDPGDAMMSLGTSGVVyaVTDKPLPDpAGAVHGFCHAL-----------PG-GWLPMGVtlsatss 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 308 LEWVRKLFWTAEtpWQILIEEARLIAPGADGVKMQCDL-------LSCQNAG-WQGVTLNTTRGHFYRAALEGLTTQLQR 379
Cdd:TIGR01312 301 LEWFRELFGKED--VEALNELAEQSPPGAEGVTFLPYLngertphLDPQARGsFIGLTHNTTRADLTRAVLEGVTFALRD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 380 NLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQYRY 459
Cdd:TIGR01312 379 SLDILREAGGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVVKQTES 458
|
...
gi 446731104 460 FYP 462
Cdd:TIGR01312 459 VLP 461
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
6-465 |
4.65e-51 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 180.22 E-value: 4.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARAST----PNASDI--AMENNTWHQWSLdailqrFADCCRQI--NSELTDCHIRGI 77
Cdd:cd07775 2 LLALDAGTGSGRAVIFDLEGNQIAVAQRewrhKEVPDVpgSMDFDTEKNWKL------ICECIREAlkKAGIAPKSIAAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 78 AVTTFGVDGALVDKQGNLLypiisWKCPRTAAVMDN-IERLIST-----QQLQAISGvGAFSFNTLYKLVWLKENHPQLL 151
Cdd:cd07775 76 STTSMREGIVLYDNEGEEI-----WACANVDARAAEeVSELKELyntleEEVYRISG-QTFALGAIPRLLWLKNNRPEIY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 152 ERAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLP 231
Cdd:cd07775 150 RKAAKITMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 232 VGIPVISAGHDTQFALFGAGA--EQNEPVLSSGTWEILmvrsAQVDTSLlsqyagstceLDSQAGL-YN----PGMqWLA 304
Cdd:cd07775 230 EGTPVVVGGGDVQLGCLGLGVvrPGQTAVLGGSFWQQE----VNTAAPV----------TDPAMNIrVNchviPDM-WQA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 305 SG-------VLEWVRKLFWTAET---------PWQILIEEARLIAPGADGvkMQCDLLSCQNAG-WQ-------GVTLN- 359
Cdd:cd07775 295 EGisffpglVMRWFRDAFCAEEKeiaerlgidAYDLLEEMAKDVPPGSYG--IMPIFSDVMNYKnWRhaapsflNLDIDp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 360 --TTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGW 437
Cdd:cd07775 373 ekCNKATFFRAIMENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAG 452
|
490 500
....*....|....*....|....*...
gi 446731104 438 YGVGEFNSPEEARAQIHYQYRYFYPQTE 465
Cdd:cd07775 453 VGAGIYSSLEEAVESLVKWEREYLPNPE 480
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
9-441 |
1.99e-50 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 177.36 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 9 LDCGATNVRAIAVN-RQGKIVARASTPnASDIAMENNTWHQ---WSLDAILQRFADCCRQINSELTDchIRGIavttfGV 84
Cdd:cd07809 5 IDLGTQSIKAVLIDaETGRVVASGSAP-HENILIDPGWAEQdpeDWWDALQAAFAQLLKDAGAELRD--VAAI-----GI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 85 DG-----ALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFnTLYKLVWLKENHPQLLERAHAWLF 159
Cdd:cd07809 77 SGqmhglVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARF-TASKLLWLKENEPEHYARIAKILL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 160 ISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQA---TGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPV 236
Cdd:cd07809 156 PHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAidpSRDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 237 ISAGHDTQFALFGAGA-EQNEPVLSSGTWEILMVRSAQV---DTSLLSQYAGSTceldsqaGLYNP---GMQWLASgVLE 309
Cdd:cd07809 236 APGEGDNMTGALGTGVvNPGTVAVSLGTSGTAYGVSDKPvsdPHGRVATFCDST-------GGMLPlinTTNCLTA-WTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 310 WVRKLF-WTAETpwqiLIEEARLIAPGADGVKMQCDL-----LSCQNAGWQ--GVTL-NTTRGHFYRAALEGLTTQLQRN 380
Cdd:cd07809 308 LFRELLgVSYEE----LDELAAQAPPGAGGLLLLPFLngertPNLPHGRASlvGLTLsNFTRANLARAALEGATFGLRYG 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446731104 381 LQMLEKIGhFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVG 441
Cdd:cd07809 384 LDILRELG-VEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
5-441 |
5.92e-50 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 176.66 E-value: 5.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNAsdIAMENNTWHQWSLDAILQRFADCCRQINSELTDC--HIRGIAVTTF 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNA--VLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLpdRVAAIGVTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GvDGA-LVDKQGNLLYPIISWKCPRTAavmDNIERLIST---QQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWL 158
Cdd:cd24121 79 G-DGTwLVDEDGRPVRDAILWLDGRAA---DIVERWQADgiaEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 159 FISSLINHRLTGEFTTDITMAGTSqMLDIQQRDFSPQILQATGIP--RRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPV 236
Cdd:cd24121 155 HCKDWLFYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 237 ISAGHDTQFALFGAGA-EQNEPVLSSGTWEILMVRSAQVDTSllSQYAGSTCELDSQaGLY---NPGMqwLASGVLEWVR 312
Cdd:cd24121 234 VLGPFDVVATALGSGAiEPGDACSILGTTGVHEVVVDEPDLE--PEGVGYTICLGVP-GRWlraMANM--AGTPNLDWFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 313 KLFWTAETP---------WQILIEEARLIAPGADGVkMQCDLLSC-----------QNAGWQGVTLNTTRGHFYRAALEG 372
Cdd:cd24121 309 RELGEVLKEgaepagsdlFQDLEELAASSPPGAEGV-LYHPYLSPagerapfvnpnARAQFTGLSLEHTRADLLRAVYEG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446731104 373 LTtqlqrnLQMLEKIGHF--KASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVG 441
Cdd:cd24121 388 VA------LAMRDCYEHMgeDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
9-465 |
9.64e-47 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 168.87 E-value: 9.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 9 LDCGATNVRAIAVN-RQGKIVARASTPNASDIAMENNTW---H--QWsLDAILQRFADCCRQinSELTDCHIRGIAVTTF 82
Cdd:cd07781 5 IDFGTQSVRAGLVDlADGEELASAVVPYPTGYIPPRPGWaeqNpaDY-WEALEEAVRGALAE--AGVDPEDVVGIGVDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGV-GAFSFNTLY-KLVWLKENHPQLLERAHAWLFI 160
Cdd:cd07781 82 SSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLAYYgGVYSSEWMWpKALWLKRNAPEVYDAAYTIVEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 161 SSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATG-----IPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIP 235
Cdd:cd07781 162 CDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDpgllkLREKLPGEVVPVGEPAGTLTAEAAERLGLPAGIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 236 VISAGHDTQFALFGAGAEQ-NEPVLSSGT--WEILMVRSAQVDTSLLSQYAGStceldsqaglYNPGMqWL------ASG 306
Cdd:cd07781 242 VAQGGIDAHMGAIGAGVVEpGTLALIMGTstCHLMVSPKPVDIPGICGPVPDA----------VVPGL-YGleagqsAVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 307 -VLEWVRKLF-----WTAETPWQILIEEARLIAPGADGVKMQ----------CDLLScQNAGWqGVTLNTTRGHFYRAAL 370
Cdd:cd07781 311 dIFAWFVRLFvppaeERGDSIYALLSEEAAKLPPGESGLVALdwfngnrtplVDPRL-RGAIV-GLTLGTTPAHIYRALL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 371 EGLT--TqlqrnLQMLEKI--GHFKASELLLVGGGS-RNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNS 445
Cdd:cd07781 389 EATAfgT-----RAIIERFeeAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYAD 463
|
490 500
....*....|....*....|
gi 446731104 446 PEEARAQIHYQYRYFYPQTE 465
Cdd:cd07781 464 IEEAADAMVRVDRVYEPDPE 483
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
6-465 |
6.08e-41 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 153.24 E-value: 6.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARA-------STPNASDiAMENNTWHQWSLdailqrFADCCRQI--NSELTDCHIRG 76
Cdd:PRK10939 5 LMALDAGTGSIRAVIFDLNGNQIAVGqaewrhlAVPDVPG-SMEFDLEKNWQL------ACQCIRQAlqKAGIPASDIAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 77 IAVTTFGVDGALVDKQGNllyPIisWKCP----RTAA-VM------DNIERlistqQLQAISGvGAFSFNTLYKLVWLKE 145
Cdd:PRK10939 78 VSATSMREGIVLYDRNGT---EI--WACAnvdaRASReVSelkelhNNFEE-----EVYRCSG-QTLALGALPRLLWLAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 146 NHPQLLERAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAA 225
Cdd:PRK10939 147 HRPDIYRQAHTITMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 226 AMLGLPVGIPVISAGHDTQFALFGAGA--EQNEPVLSSGTW-EILMVRSAQVDTSL-----------LSQYAGSTcelds 291
Cdd:PRK10939 227 AETGLRAGTPVVMGGGDVQLGCLGLGVvrPGQTAVLGGTFWqQVVNLPAPVTDPNMnirinphvipgMVQAESIS----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 292 qaglYNPGMqwlasgVLEWVRKLFWTAET---------PWQILIEEARLIAPGADGV------KMqcDLLSCQNAGWQGV 356
Cdd:PRK10939 302 ----FFTGL------TMRWFRDAFCAEEKllaerlgidAYSLLEEMASRVPVGSHGIipifsdVM--RFKSWYHAAPSFI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 357 TLN-----TTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAG 431
Cdd:PRK10939 370 NLSidpekCNKATLFRALEENAAIVSACNLQQIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALG 449
|
490 500 510
....*....|....*....|....*....|....
gi 446731104 432 AALFGWYGVGEFNSPEEARAQIHYQYRYFYPQTE 465
Cdd:PRK10939 450 CAIAAGVGAGIYSSLAETGERLVRWERTFEPNPE 483
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
5-435 |
1.30e-39 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 148.14 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQ-GKIVARASTPNASDIAMENNTWHQWSLDAILQRFADCCRQINSELtDCHIRGIAVTT-- 81
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLEsGRILESVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREY-LSDVTGIGITGqm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 82 FGVdgALVDKQGNLLYPIISWKCPRTAAVMDN-----IERLISTQQLQAISGVGAFsfnTLYklvWLKENHPqLLERAHA 156
Cdd:cd07777 80 HGI--VLWDEDGNPVSPLITWQDQRCSEEFLGglstyGEELLPKSGMRLKPGYGLA---TLF---WLLRNGP-LPSKADR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 157 WLFISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSaaamlgLPVGI 234
Cdd:cd07777 151 AGTIGDYIVARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSA------LPKGI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 235 PVISAGHDTQFALFGAGAEQ-NEPVLSSGTweilmvrSAQVdtSLLSQYAGSTCELDSQ-----------AGLynPG--- 299
Cdd:cd07777 225 PVYVALGDNQASVLGSGLNEeNDAVLNIGT-------GAQL--SFLTPKFELSGSVEIRpffdgryllvaASL--PGgra 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 300 MQWLASGVLEWVRKLFWT--AETPWQILIEEARLIAPGAdgvkMQCDLL-------SCQNAGWQGVTL-NTTRGHFYRAA 369
Cdd:cd07777 294 LAVLVDFLREWLRELGGSlsDDEIWEKLDELAESEESSD----LSVDPTffgerhdPEGRGSITNIGEsNFTLGNLFRAL 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446731104 370 LEGLTTQLQRNLQMLEKIGHfKASELLLVGGGSR-NTLWNQIKANMLDIPVKVLDDAETTVAGAALF 435
Cdd:cd07777 370 CRGIAENLHEMLPRLDLDLS-GIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALL 435
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
5-279 |
2.06e-36 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 138.93 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNAS---------DIAmenNTWhQWSLDAiLQRFADccrqinseltDCHIR 75
Cdd:cd07772 1 VIAVFDIGKTNKKLLLFDENGEVLAERSTPNPEieedgypceDVE---AIW-EWLLDS-LAELAK----------RHRID 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 76 GIAVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSfNTLYKLVWLKENHPQLLERAH 155
Cdd:cd07772 66 AINFTTHGATFALLDENGELALPVYDYEKPIPDEINEAYYAERGPFEETGSPPLPGGL-NLGKQLYWLKREKPELFARAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 156 AWLFISSLINHRLTGEFTTDITMAGT-SQMLDIQQRDFSPqILQATGIpRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGI 234
Cdd:cd07772 145 TILPLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEYSS-LVKKEGW-DKLFPPLRKAWEVLGPLRPDLARRTGLPKDI 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446731104 235 PVISAGHDTQFAL--FGAGAEQNEPVLSSGTWEILMVRSAQVDTSLL 279
Cdd:cd07772 223 PVGCGIHDSNAALlpYLAAGKEPFTLLSTGTWCIAMNPGNDLPLTEL 269
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
6-471 |
1.38e-35 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 137.98 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARASTPNAS----------DiAMEnntwhqwsldaILQRFADCCRQI--NSELTDCH 73
Cdd:cd07769 2 ILAIDQGTTSTRAILFDEDGNIVASAQKEHEQiypqpgwvehD-PEE-----------IWENTLEVIREAlaKAGISASD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 74 IRGIAVT----TFgvdgALVDKQ-GNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISG--VGA-FSFNtlyKLVWLKE 145
Cdd:cd07769 70 IAAIGITnqreTT----VVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEERIREKTGlpLDPyFSAT---KIKWILD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 146 NHPQLLERAHA--WLF--ISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGT 219
Cdd:cd07769 143 NVPGARERAERgeLLFgtIDTWLIWKLTGgkVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 220 LQNSaaamlGLPVGIPVISAGHDTQFALFGAGAEQ-------------------NEPVLSSGtweilmvrsaqvdtSLLS 280
Cdd:cd07769 223 TDPE-----GLGAGIPIAGILGDQQAALFGQGCFEpgmakntygtgcfllmntgEKPVPSKN--------------GLLT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 281 ----------QYA--GSTceldsqaglynpgmqwLASG-VLEWVRKLFWtaetpwqiLIEEARLIAPGADGVKmqcdlls 347
Cdd:cd07769 284 tiawqiggkvTYAleGSI----------------FIAGaAIQWLRDNLG--------LIEDAAETEELARSVE------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 348 cQNAG--------------WQ--------GVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNT 405
Cdd:cd07769 333 -DNGGvyfvpafsglgapyWDpdargaivGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANN 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446731104 406 LWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQyRYFYPQTEPEFIEE 471
Cdd:cd07769 412 FLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVD-KRFEPSMDEEERER 476
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
47-419 |
7.62e-33 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 129.84 E-value: 7.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 47 HQWSLDAILQRFADCCRQINSEltDCHIRGIAVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISTQQLQAI 126
Cdd:PRK10640 31 DTWDVDSLESAIRLGLNKVCEE--GIRIDSIGIDTWGVDYVLLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 127 SGVGAFSFNTLYKLVWLKENHPQLLER-AHAwLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRR 205
Cdd:PRK10640 109 SGIQFLPFNTLYQLRALTEQQPELIAQvAHA-LLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 206 LFPRLVEAGEQIGTLQNsaaamlglPVG--IPVIS-AGHDTQFALFGAG-AEQNEPVLSSGTWEILMVRSAQVDTSLLSQ 281
Cdd:PRK10640 188 WFGRPTHPGNVIGHWIC--------PQGneIPVVAvASHDTASAVIASPlNDSDAAYLSSGTWSLMGFESQTPFTNDTAL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 282 YAGSTCE---------LDSQAGLynpgmqWLASGVLEwVRKLfwtaeTPWQILIEEAR-------LIAPGAD----GVKM 341
Cdd:PRK10640 260 AANITNEggaegryrvLKNIMGL------WLLQRVLQ-ERQI-----TDLPALIAATAalpacrfLINPNDDrfinPPSM 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446731104 342 QCDLLS-CQNAGwQGVTlnTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPV 419
Cdd:PRK10640 328 CSEIQAaCRETA-QPVP--ESDAELARCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLCADACGIRV 403
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-467 |
8.03e-29 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 118.63 E-value: 8.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 1 MKQeVILVLDCGATNVRAIAVNRQGKIVARAS------TPNASdiamenntW--HqwslDA--ILQRFADCCRQ--INSE 68
Cdd:COG0554 1 MKK-YILAIDQGTTSTRAILFDRDGNIVAVAQreftqiYPQPG--------WveH----DPeeIWESVLAVIREalAKAG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 69 LTDCHIRGIAVT----TFgvdgaLV-DKQ-GNLLYPIISWKCPRTAAVmdnIERLISTQQLQAI------------SGVg 130
Cdd:COG0554 68 ISAEDIAAIGITnqreTT-----VVwDRKtGKPLYNAIVWQDRRTADI---CEELKADGLEDLIrektglvldpyfSAT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 131 afsfntlyKLVWLKENHPQLLERAHA--WLF--ISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPQILQATGIPR 204
Cdd:COG0554 139 --------KIKWILDNVPGARERAEAgeLLFgtIDSWLIWKLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 205 RLFPRLVEAGEQIGTLQNSaaamlGLPVGIPVIS-AGhDTQFALFGAGAEQ-------------------NEPVLSSGtw 264
Cdd:COG0554 211 SMLPEVRPSSEVFGETDPD-----LFGAEIPIAGiAG-DQQAALFGQACFEpgmakntygtgcfllmntgDEPVRSKN-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 265 eilmvrsaqvdtSLLS----------QYA--------GSTceldsqaglynpgMQWLASGvLEwvrklfwtaetpwqiLI 326
Cdd:COG0554 283 ------------GLLTtiawglggkvTYAlegsifvaGAA-------------VQWLRDG-LG---------------LI 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 327 EEARLIAPGADGVKmqcdllscQNAG--------------WQ--------GVTLNTTRGHFYRAALEGLTTQLQRNLQML 384
Cdd:COG0554 322 DSAAESEALARSVE--------DNGGvyfvpaftglgapyWDpdargaifGLTRGTTRAHIARAALESIAYQTRDVLDAM 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 385 EKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHyQYRYFYPQT 464
Cdd:COG0554 394 EADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEELAALWK-VDRRFEPQM 472
|
...
gi 446731104 465 EPE 467
Cdd:COG0554 473 DEE 475
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
9-414 |
6.10e-28 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 116.22 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 9 LDCGATNVRAIAVNRQGKIVA------RASTPNASDIAMENNTWHQwSLDAILQRFADccrqiNSELTDCHIRGIAVTTF 82
Cdd:PRK15027 5 IDLGTSGVKVILLNEQGEVVAsqteklTVSRPHPLWSEQDPEQWWQ-ATDRAMKALGD-----QHSLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GvdGALVDKQGNLLYPIISWKCPRTAAVMDNIERLIStqQLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISS 162
Cdd:PRK15027 79 G--ATLLDAQQRVLRPAILWNDGRCAQECALLEARVP--QSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 163 LINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPvGIPVISAGHD 242
Cdd:PRK15027 155 YLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMA-TVPVVAGGGD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 243 TQFALFGAG-AEQNEPVLSSGTWEILMVrsaqVDTSLLSQ---YAGSTCE-LDSQAGLYNPGMQwlASGVLEWVRKLFWT 317
Cdd:PRK15027 234 NAAGAVGVGmVDANQAMLSLGTSGVYFA----VSEGFLSKpesAVHSFCHaLPQRWHLMSVMLS--AASCLDWAAKLTGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 318 AETPwqILIEEARLIAPGADGV----KMQCDLLSCQNAGWQGVTLNTTRGH----FYRAALEGLTTQLQRNLQMLEKIGh 389
Cdd:PRK15027 308 SNVP--ALIAAAQQADESAEPVwflpYLSGERTPHNNPQAKGVFFGLTHQHgpneLARAVLEGVGYALADGMDVVHACG- 384
|
410 420
....*....|....*....|....*
gi 446731104 390 FKASELLLVGGGSRNTLWNQIKANM 414
Cdd:PRK15027 385 IKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
6-471 |
1.81e-27 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 114.97 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARASTPnasdIAMENNT--WHQWSLDAILQRFADCCRQI--NSELTDCHIRGIAVTT 81
Cdd:cd07793 2 ILAVDVGTTNIRCHIFDKKGKIIGSSSEK----VEVLYPEpgWVEIDPEELWQQFVKVIKEAlkNAGLTPEDIAAIGIST 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 82 FGVDGALVDKQ-GNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVG-------------AFSFNT---LYKLVWLK 144
Cdd:cd07793 78 QRNTFLTWDKKtGKPLHNFITWQDLRAAELCESWNRSLLLKALRGGSKFLhfltrnkrflaasVLKFSTahvSIRLLWIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 145 ENHPQLLERA--HAWLF--ISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIG 218
Cdd:cd07793 158 QNNPELKEAAekGELLFgtIDTWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSGDFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 219 TLQNSaaamlGLPVGIPVISAGHDTQFALFGAGaeqnepVLSSGTWEILMVRSAQVDTSLlsqyaGSTCeLDSQAGLYnP 298
Cdd:cd07793 238 STDPS-----IFGAEIPITAVVADQQAALFGEC------CFDKGDVKITMGTGTFIDINT-----GSKP-HASVKGLY-P 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 299 GMQW--------LASG-------VLEWVRK--LFwtaETPWQilIEEARLIAPGADGV-------KMQC---DLLSCqnA 351
Cdd:cd07793 300 LVGWkiggeityLAEGnasdtgtVIDWAKSigLF---DDPSE--TEDIAESVEDTNGVyfvpafsGLQApynDPTAC--A 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 352 GWQGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAG 431
Cdd:cd07793 373 GFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALG 452
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446731104 432 AALFGWYGVGEFNSPEEARAqIHYQYRYFYPQTEPEFIEE 471
Cdd:cd07793 453 AAFLAGLASGIWKSKEELKK-LRKIEKIFEPKMDNEKREE 491
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
3-467 |
4.09e-25 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 107.75 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 3 QEVILVLDCGATNVRAIAVNRQGKIVArastpnASDIAMENNTWHQ-WS-------LDAILQRFADCCRQINSELTDCHI 74
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVS------SHQIPHEQITPHPgWLehdpeeiLRNVYKCMNEAIKKLREKGPSFKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 75 RGIAVTTFGVDGALVDKQ-GNLLYPIISWKCPRTAAVMDNIERLISTQQL-QAISGVGAFSFNTLYKLVWLKENHPQL-- 150
Cdd:PTZ00294 75 KAIGITNQRETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFfQKITGLPISTYFSAFKIRWMLENVPAVkd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 151 -LERAHAwLF--ISSLINHRLTGE--FTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAA 225
Cdd:PTZ00294 155 aVKEGTL-LFgtIDTWLIWNLTGGksHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGEAV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 226 AMLglpVGIPVISAGHDTQFALFGAGAEQ-------------------NEPVLSSGTweILMVRSAQVDTSLLSQYA--G 284
Cdd:PTZ00294 234 PLL---EGVPITGCIGDQQAALIGHGCFEkgdakntygtgcfllmntgTEIVFSKHG--LLTTVCYQLGPNGPTVYAleG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 285 STceldSQAGlynpgmqwlaSGVlEWVRKLFWTAETPWQI--LIEEAR-------------LIAP----GADGVKMqcdl 345
Cdd:PTZ00294 309 SI----AVAG----------AGV-EWLRDNMGLISHPSEIekLARSVKdtggvvfvpafsgLFAPywrpDARGTIV---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 346 lscqnagwqGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDA 425
Cdd:PTZ00294 370 ---------GMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMA 440
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446731104 426 ETTVAGAALFGWYGVGEFNSPEEARAQIHYQYRYFYPQTEPE 467
Cdd:PTZ00294 441 ETTALGAALLAGLAVGVWKSLEEVKKLIRRSNSTFSPQMSAE 482
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
6-452 |
8.39e-25 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 106.81 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARAST------PNASdiamenntWHQWSLDAILQRFADCCRQI--NSELTDCHIRGI 77
Cdd:cd07786 2 ILAIDQGTTSSRAILFDHDGNIVAVAQReftqiyPKPG--------WVEHDPEEIWESQLAVAREAlaKAGIRASDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 78 AVT----TfgvdgALV-DKQ-GNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGV---GAFSfNTlyKLVWLKENHP 148
Cdd:cd07786 74 GITnqreT-----TVVwDREtGKPVYNAIVWQDRRTADICEELKAEGHEEMIREKTGLvldPYFS-AT--KIRWILDNVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 149 QLLERAHA--WLF--ISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQN 222
Cdd:cd07786 146 GARERAERgeLAFgtIDSWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFGYTDP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 223 SaaamlGLPVGIPVISAGHDTQFALFGAGAEQ-------------------NEPVLSS----GT--WEIlmvrSAQVdts 277
Cdd:cd07786 226 D-----LLGAEIPIAGIAGDQQAALFGQACFEpgmakntygtgcfmlmntgEKPVRSKngllTTiaWQL----GGKV--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 278 llsQYA--GStceldsqagLYNPG--MQWLASGVLewvrklfwtaetpwqiLIEEARLIAPGADGVKmqcdllscQNAG- 352
Cdd:cd07786 294 ---TYAleGS---------IFIAGaaVQWLRDGLG----------------LIESAAETEALARSVP--------DNGGv 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 353 -------------WQ--------GVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIK 411
Cdd:cd07786 338 yfvpaftglgapyWDpdargaifGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQ 417
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446731104 412 ANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQ 452
Cdd:cd07786 418 ADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKL 458
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
9-467 |
2.07e-20 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 94.00 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 9 LDCGATNVRAIAVNRQGKIVARAST------PNASdiamenntWHQWSLDAILQRFADCCRQInseltdchIRGIAVTTF 82
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVeftqiyPQAG--------WVEHDPMEILESVLTCIAKA--------LEKAAAKGH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 83 GVDGALV---------------DKQGNLLYPIISWKCPRTAAVMDNIERLIS--TQQLQAISGVGAFSFNTLYKLVWLKE 145
Cdd:PLN02295 69 NVDSGLKaigitnqrettvawsKSTGRPLYNAIVWMDSRTSSICRRLEKELSggRKHFVETCGLPISTYFSATKLLWLLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 146 NHPQL---LERAHAwLF--ISSLINHRLTG-----EFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGE 215
Cdd:PLN02295 149 NVDAVkeaVKSGDA-LFgtIDSWLIWNLTGgasggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 216 QIGTLQNsaaamlGLPV-GIPVISAGHDTQFALFGAGAEQNEPVLSSGTWEILMVRSAQVDTS----LLS---------- 280
Cdd:PLN02295 228 VIGTIAK------GWPLaGVPIAGCLGDQHAAMLGQRCRPGEAKSTYGTGCFILLNTGEEVVPskhgLLTtvayklgpda 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 281 --QYA--GSTceldSQAGLynpGMQWLASGVLewvrklfwtaetpwqiLIEEARLIAPGADgvkmqcdllSCQNAG---- 352
Cdd:PLN02295 302 ptNYAleGSV----AIAGA---AVQWLRDNLG----------------IIKSASEIEALAA---------TVDDTGgvyf 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 353 -----------WQ--------GVTLNTTRGHFYRAALEGLTTQLQRNLQMLEK----IGHFKASELLLV-GGGSRNTLWN 408
Cdd:PLN02295 350 vpafsglfaprWRddargvcvGITRFTNKAHIARAVLESMCFQVKDVLDAMRKdageEKSHKGLFLLRVdGGATANNLLM 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 409 QIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFnSPEEARAQIHYQYR-YFYPQTEPE 467
Cdd:PLN02295 430 QIQADLLGSPVVRPADIETTALGAAYAAGLAVGLW-TEEEIFASEKWKNTtTFRPKLDEE 488
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
4-467 |
2.13e-20 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 93.74 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 4 EVILVLDCGATNVRAIAVNRQGKIVA------RASTPNASdiamenntWHQWSLDAILQRFADC----CRQINSE-LTDC 72
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVAshqvehKQIYPKPG--------WVEHDPMEILESVYECieeaVEKLKALgISPS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 73 HIRGIAVT----TfgvdgaLV--DKQ-GNLLYPIISWKCPRTAAVmdnIERLIST-----QQLQAISGVGAFSFNTLYKL 140
Cdd:cd07792 73 DIKAIGITnqreT------TVvwDKStGKPLYNAIVWLDTRTSDT---VEELSAKtpggkDHFRKKTGLPISTYFSAVKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 141 VWLKENHP---QLLERAHAwLF--ISSLINHRLTGE-----FTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRL 210
Cdd:cd07792 144 RWLLDNVPevkKAVDDGRL-LFgtVDSWLIWNLTGGknggvHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 211 VEAGEQIGTLQNSAAAmlglpvGIPvISA--GhDTQFALFG-----AGAEQN--------------EPVLSSGtweilmv 269
Cdd:cd07792 223 RSSSEVYGKIASGPLA------GVP-ISGclG-DQQAALVGqgcfkPGEAKNtygtgcfllyntgeEPVFSKH------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 270 rsaqvdtSLLS------------QYA--GSTceldSQAGLynpGMQWLasgvlewvRKLFwtaetpwqILIEEARLIAPG 335
Cdd:cd07792 288 -------GLLTtvayklgpdappVYAleGSI----AIAGA---AVQWL--------RDNL--------GIISSASEVETL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 336 ADGVKmqcdllscQNAG--------------WQ--------GVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKAS 393
Cdd:cd07792 338 AASVP--------DTGGvyfvpafsglfapyWRpdargtivGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLT 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446731104 394 ELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQYRYFYPQTEPE 467
Cdd:cd07792 410 SLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEE 483
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
258-436 |
3.50e-18 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 82.37 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 258 VLSSGTWEILMV--RSAQVDT-SLLSQYAGStcelDSQAGLYNPGMQWLASGVLEWVRKlFWTAETPWQI-----LIEEA 329
Cdd:pfam02782 2 AISAGTSSFVLVetPEPVLSVhGVWGPYTNE----MLPGYWGLEGGQSAAGSLLAWLLQ-FHGLREELRDagnveSLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 330 RLIAPGADGVKMQCDL-LSCQNA---------GWQGVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVG 399
Cdd:pfam02782 77 AALAAVAPAGGLLFYPdFSGNRApgadpgargSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVSG 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 446731104 400 GGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFG 436
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLA 193
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-467 |
3.43e-13 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 71.39 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 1 MKQEVILVLDCGATNVRAIAVNRQGKIVARAST------PNASDIamENNTWHQWS--LDAILQRFADCcrQINSEltdc 72
Cdd:PRK00047 2 MMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKeftqifPQPGWV--EHDPNEIWAsqLSVIAEALAKA--GISPD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 73 HIRGIAVT----TfgvdgALV-DKQ-GNLLYPIISWKCPRTAAVMDNIERLISTQQLQAISGVGAFSFNTLYKLVWLKEN 146
Cdd:PRK00047 74 QIAAIGITnqreT-----TVVwDKEtGRPIYNAIVWQDRRTADICEELKRDGYEDYIREKTGLVIDPYFSGTKIKWILDN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 147 HPQLLERAHA--WLF--ISSLINHRLTGEFT--TDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTl 220
Cdd:PRK00047 149 VEGARERAEKgeLLFgtIDTWLVWKLTGGKVhvTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGK- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 221 qnsAAAMLGLPVGIPVISAGHDTQFALFG-----AGAEQNepvlSSGTWE-ILM------VRSaqvDTSLLSQYAgstCE 288
Cdd:PRK00047 228 ---TNPYGFFGGEVPIAGIAGDQQAALFGqlcfePGMAKN----TYGTGCfMLMntgekaVKS---ENGLLTTIA---WG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 289 LDSQAGLYNPGMQWLASGVLEWVR---KLFWTAETpwqilIEEARLIAPGADGVKMQCDLlscqnAG-----WQ------ 354
Cdd:PRK00047 295 IDGKVVYALEGSIFVAGSAIQWLRdglKIISDASD-----SEALARKVEDNDGVYVVPAF-----TGlgapyWDsdarga 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 355 --GVTLNTTRGHFYRAALEGLTTQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGA 432
Cdd:PRK00047 365 ifGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGA 444
|
490 500 510
....*....|....*....|....*....|....*
gi 446731104 433 ALFGWYGVGEFNSPEEARAQIHYQYRyFYPQTEPE 467
Cdd:PRK00047 445 AYLAGLAVGFWKDLDELKEQWKIDRR-FEPQMDEE 478
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
9-464 |
6.84e-11 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 64.18 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 9 LDCGATNVRAIAVN-RQGKIVARASTPNASDIAMENNTWHQWSLDaILQRFADCCRQINSEltdCHIRGIAVTTFGVDG- 86
Cdd:cd07768 5 VDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSSKKSWKFWQKSTE-IIKALQKCVQKLNIR---EGVDAYEVKGCGVDAt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 87 ---ALVDKQGN---LLYP------IISWKcprTAAVMDNIERLIST--QQLQAISGvGAFSFNTLY-KLVWLKENHPQLL 151
Cdd:cd07768 81 cslAIFDREGTplmALIPypnednVIFWM---DHSAVNEAQWINMQcpQQLLDYLG-GKISPEMGVpKLKYFLDEYSHLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 152 ERAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGI------PRRLFPRLVEAGEQIGTLQNSAA 225
Cdd:cd07768 157 DKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPrlehltTTKNLPSNVPIGTTSGVALPEMA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 226 AMLGLPVGIPVISAGHDTQFALFGAGAEQNEP--VLSSGTWEILMV--RSAQ--------VDTSLLSQY----AGSTCEL 289
Cdd:cd07768 237 EKMGLHPGTAVVVSCIDAHASWFAVASPHLETslFMIAGTSSCHMYgtTISDripgvwgpFDTIIDPDYsvyeAGQSATG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 290 DSQAGLYNPGMqwLASGVLEWVRKlfwtAETPWQILIEEARLIAPGADGvkmQCDLLSCQ--------------NAGWQG 355
Cdd:cd07768 317 KLIEHLFESHP--CARKFDEALKK----GADIYQVLEQTIRQIEKNNGL---SIHILTLDmffgnrsefadprlKGSFIG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 356 VTLNTTRGHF---YRAALEGLTTQLQRNLQMLEKIGhFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGA 432
Cdd:cd07768 388 ESLDTSMLNLtykYIAILEALAFGTRLIIDTFQNEG-IHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGA 466
|
490 500 510
....*....|....*....|....*....|....*
gi 446731104 433 ALFGWYGVGEF---NSPEEARAQIHYQYRYFYPQT 464
Cdd:cd07768 467 AVLAKVAAGKKqlaDSITEADISNDRKSETFEPLA 501
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
199-453 |
2.09e-07 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 53.31 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 199 ATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHDTQFALFGAGAEQNE--PVLSSGTWEILMVRSA---- 272
Cdd:PRK04123 231 ARGLRDKLFTETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGAEPGTlvKVMGTSTCDILLADKQravp 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 273 ----QVDTSLLSQYAGstceldSQAGLynpgmqwlaSGV---LEWVRKLFWTAETPWQI----------LIEEARLIAPG 335
Cdd:PRK04123 311 gicgQVDGSIVPGLIG------YEAGQ---------SAVgdiFAWFARLLVPPEYKDEAeargkqllelLTEAAAKQPPG 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 336 ADGVkMQCDLLSCQ-----NAGWQGV----TLNTTRGHFYRAALE----GLTTQLQRnlqmlekighFKAS-----ELLL 397
Cdd:PRK04123 376 EHGL-VALDWFNGRrtplaDQRLKGVitglTLGTDAPDIYRALIEatafGTRAIMEC----------FEDQgvpveEVIA 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446731104 398 VGGGSR-NTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQI 453
Cdd:PRK04123 445 AGGIARkNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAM 501
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
366-449 |
8.02e-04 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 41.75 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 366 YRAALEGLTTQLQRNLQMLEKIGHfKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNS 445
Cdd:cd07782 419 YLATLQALAYGTRHIIEAMNAAGH-KIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPS 497
|
....
gi 446731104 446 PEEA 449
Cdd:cd07782 498 LWDA 501
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
366-453 |
8.45e-04 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 41.77 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 366 YRAALEGlttqlqrnlQML------EKIG-HFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWY 438
Cdd:cd07776 402 VRAVVES---------QFLsmrlhaERLGsDIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAH 472
|
90
....*....|....*
gi 446731104 439 GVGEFNSPEEARAQI 453
Cdd:cd07776 473 GLLCAGSGDFSPEFV 487
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
5-97 |
1.90e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 40.27 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 5 VILVLDCGATNVRAIAVNRQGKIVARASTPNASDIamenntwhqwSLDAILQRFADCCRQI--NSELTDCHIRGIAVTTF 82
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGA----------GPEAVLEAIAELIEELlaEAGISRGRILGIGIGVP 75
|
90
....*....|....*
gi 446731104 83 GVdgalVDKQGNLLY 97
Cdd:COG1940 76 GP----VDPETGVVL 86
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
6-97 |
8.38e-03 |
|
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466918 [Multi-domain] Cd Length: 294 Bit Score: 38.31 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARASTPnasdiamennTWHQWSLDAILQRFAdccRQINSELTDCHIRGIAVTTFGVd 85
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDSVP----------TPASKGGDAILERLL---EIIAELKEKYDIEGIGISSAGQ- 67
|
90
....*....|...
gi 446731104 86 galVD-KQGNLLY 97
Cdd:cd24068 68 ---VDpKTGEVIY 77
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
6-101 |
8.52e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 38.05 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446731104 6 ILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMEnntwHQWSLDAILQRFADCCRQINSELTdchirgIAVTTFGVD 85
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRGKGGPSNPASVG----IEEAKENLKEAVREALSQAGSLGE------IDAICLGLA 70
|
90
....*....|....*.
gi 446731104 86 GALVDKQGNLLYPIIS 101
Cdd:cd24007 71 GIDSEEDRERLRSALK 86
|
|
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