|
Name |
Accession |
Description |
Interval |
E-value |
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1-367 |
6.05e-88 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 269.47 E-value: 6.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 1 MKSYIVVGAGILGASTAYHLAKAGANVTIVDRQQVGQ-ATDAAAGIVCPWLSQRRNKAWYRIVKGGARYYssliQQLEED 79
Cdd:COG0665 2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSgASGRNAGQLRPGLAALADRALVRLAREALDLW----RELAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 80 GETDTGYNRVGAISLHTDEKKLDQMEERAykrrEDAPEIG-EITRLSAEETKKLFPALSEE--YSSVHISGAARVNGRLL 156
Cdd:COG0665 78 LGIDCDFRRTGVLYLARTEAELAALRAEA----EALRALGlPVELLDAAELREREPGLGSPdyAGGLYDPDDGHVDPAKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 157 RNALISAAKKHGATFIKGDAV--LVCEGNHINGVKVNDETILAEKVIVTAGAWAKEILNPLGINFLVTFQKGQIVHLQME 234
Cdd:COG0665 154 VRALARAARAAGVRIREGTPVtgLEREGGRVTGVRTERGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVTEPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 235 nTATENMPVVMPPNDqYILTFDNGHVVIGATHEnDTGFDHRVTAGGLNEVFQKALTVAPGLENATMLETRVGFRPFTPGF 314
Cdd:COG0665 234 -PDLPLRPVLDDTGV-YLRPTADGRLLVGGTAE-PAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDG 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1033168231 315 LPVIGPLPNFEGILVANGLGASGLTAGPYLGSELAKLALGQSIELDLNDYDVA 367
Cdd:COG0665 311 LPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAPFSPD 363
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
5-351 |
1.50e-61 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 201.09 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQQV--GQATDAAAGIVCPWLSQRRNKAWYRIVKGGARyyssLIQQLEEDGET 82
Cdd:pfam01266 3 VVIGGGIVGLSTAYELARRGLSVTLLERGDDpgSGASGRNAGLIHPGLRYLEPSELARLALEALD----LWEELEEELGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 83 DTGYNRVGAISLHTDEKKLDQMEERAYKRREDAPEigeiTRLSAEETKKLFPALSEEYSSVHISGAARVNGRLLRNALIS 162
Cdd:pfam01266 79 DCGFRRCGVLVLARDEEEEALEKLLAALRRLGVPA----ELLDAEELRELEPLLPGLRGGLFYPDGGHVDPARLLRALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 163 AAKKHGATFIKGDAVLVCEgnHINGVKVNDETILAEKVIVTAGAWAKEILNPlGINFLVTFQKGQIVHLQMENTATENMP 242
Cdd:pfam01266 155 AAEALGVRIIEGTEVTGIE--EEGGVWGVVTTGEADAVVNAAGAWADLLALP-GLRLPVRPVRGQVLVLEPLPEALLILP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 243 VVMPPNDQ---YILTFDNGHVVIGATHENDTGFDHRVTAGGLNEVFQKALTVAPGLenATMLETRVGFRPfTPGFLPVIG 319
Cdd:pfam01266 232 VPITVDPGrgvYLRPRADGRLLLGGTDEEDGFDDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLRP-LPDGLPIIG 308
|
330 340 350
....*....|....*....|....*....|..
gi 1033168231 320 PlPNFEGILVANGLGASGLTAGPYLGSELAKL 351
Cdd:pfam01266 309 R-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
5-367 |
3.43e-21 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 94.10 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQ-QVGQATDAA-AGIVCP-----------------WLSQRR----------- 54
Cdd:PRK00711 4 VVLGSGVIGVTSAWYLAQAGHEVTVIDRQpGPALETSFAnAGQISPgyaapwaapgvplkaikWLFQRHaplairpdgdp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 55 -------------NKAWYRIVKggAR-----YYS-SLIQQLEEdgETDTGYN--RVGAISLHTDEKKLDQMEER-AYKRR 112
Cdd:PRK00711 84 fqlrwmwqmlrncTASRYAVNK--SRmvrlaEYSrDCLKALRA--ETGIQYEgrQGGTLQLFRTQQQLDAAAKDiAVLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 113 EDAP-EIgeitrLSAEETKKLFPALSEeySSVHISGAARVNG------RLLRNALISAAKKHGATFIKGDAV--LVCEGN 183
Cdd:PRK00711 160 AGVPyEL-----LDRDELAAVEPALAG--VRHKLVGGLRLPNdetgdcQLFTQRLAAMAEQLGVKFRFNTPVdgLLVEGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 184 HINGVKVNDETILAEKVIVTAGAWAKEILNPLGINFLVTFQKGQIVHLQMENTATEnmPV--VMppnDQyilTFdngHVV 261
Cdd:PRK00711 233 RITGVQTGGGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTVPITDEDRA--PVstVL---DE---TY---KIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 262 IgathendTGFDHRVTAGGLNEV--FQKALTVA-------------PGLENATMLETRVGFRPFTPGFLPVIGPLPnFEG 326
Cdd:PRK00711 302 I-------TRFDDRIRVGGMAEIvgFDLRLDPArretlemvvrdlfPGGGDLSQATFWTGLRPMTPDGTPIVGATR-YKN 373
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1033168231 327 ILVANGLGASGLTAGPYLGSELAKLALGQSIELDLNDYDVA 367
Cdd:PRK00711 374 LWLNTGHGTLGWTMACGSGQLLADLISGRKPAIDADDLSVA 414
|
|
| MnmC_Cterm |
TIGR03197 |
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ... |
16-362 |
1.07e-15 |
|
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274478 [Multi-domain] Cd Length: 381 Bit Score: 77.69 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 16 TAYHLAKAGANVTIVDRQ-QVGQATDA-AAGIVCPWLSQRRNkAWYRIVKGGARYYSSLIQQLEEDGETdTGYNRVGAIS 93
Cdd:TIGR03197 1 TAYSLARRGWQVTLYEQDeAPAQGASGnPQGALYPLLSADDN-PLSRFFLAAFLYARRFYRQLAEAGFP-FDHEWCGVLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 94 LHTDEKKLDQMEERAykRREDAPEigEITR-LSAEETKKLFpALSEEYSSVHISGAARVNGRLLRNALISAAkkhgatfi 172
Cdd:TIGR03197 79 LAYDEKEAERLQKLL--EQLGFPE--ELARwVDAEQASQLA-GIPLPYGGLFFPQGGWLSPPQLCRALLAHA-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 173 kGDAVLVCEGNHINGVK----------VNDETILAEKVIVTAGAWAKEiLNPLGiNFLVTFQKGQIVHLQmENTATENMP 242
Cdd:TIGR03197 146 -GIRLTLHFNTEITSLErdgegwqlldANGEVIAASVVVLANGAQAPQ-LAQTA-HLPLRPVRGQVSHLP-ATEALSALK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 243 VVMPpNDQYILTFDNGHVVIGATHE---NDTGF---DHRvtagglnEVFQKALTVAPGLENATMLET-----RVGFRPFT 311
Cdd:TIGR03197 222 TVLC-YDGYLTPANNGEHCIGASYDrndDDLALreaDHA-------ENLERLAECLPALAWASEVDIsalqgRVGVRCAS 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033168231 312 PGFLPVIGPLPNFE-------------------------GILVANGLGASGLTAGPyLGSE-LAKLALGQSIELDLN 362
Cdd:TIGR03197 294 PDHLPLVGAVPDFEaikeayaelakdknrpiaepapyypGLYVLGGLGSRGLTSAP-LAAEiLAAQICGEPLPLERD 369
|
|
| HSD10-like_SDR_c |
cd05371 |
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ... |
8-47 |
4.85e-03 |
|
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187629 [Multi-domain] Cd Length: 252 Bit Score: 38.04 E-value: 4.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1033168231 8 GAGILGASTAYHLAKAGANVTIVDRQQVGQATDAAAGIVC 47
Cdd:cd05371 10 GASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDNC 49
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1-367 |
6.05e-88 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 269.47 E-value: 6.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 1 MKSYIVVGAGILGASTAYHLAKAGANVTIVDRQQVGQ-ATDAAAGIVCPWLSQRRNKAWYRIVKGGARYYssliQQLEED 79
Cdd:COG0665 2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSgASGRNAGQLRPGLAALADRALVRLAREALDLW----RELAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 80 GETDTGYNRVGAISLHTDEKKLDQMEERAykrrEDAPEIG-EITRLSAEETKKLFPALSEE--YSSVHISGAARVNGRLL 156
Cdd:COG0665 78 LGIDCDFRRTGVLYLARTEAELAALRAEA----EALRALGlPVELLDAAELREREPGLGSPdyAGGLYDPDDGHVDPAKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 157 RNALISAAKKHGATFIKGDAV--LVCEGNHINGVKVNDETILAEKVIVTAGAWAKEILNPLGINFLVTFQKGQIVHLQME 234
Cdd:COG0665 154 VRALARAARAAGVRIREGTPVtgLEREGGRVTGVRTERGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVTEPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 235 nTATENMPVVMPPNDqYILTFDNGHVVIGATHEnDTGFDHRVTAGGLNEVFQKALTVAPGLENATMLETRVGFRPFTPGF 314
Cdd:COG0665 234 -PDLPLRPVLDDTGV-YLRPTADGRLLVGGTAE-PAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDG 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1033168231 315 LPVIGPLPNFEGILVANGLGASGLTAGPYLGSELAKLALGQSIELDLNDYDVA 367
Cdd:COG0665 311 LPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAPFSPD 363
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
5-351 |
1.50e-61 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 201.09 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQQV--GQATDAAAGIVCPWLSQRRNKAWYRIVKGGARyyssLIQQLEEDGET 82
Cdd:pfam01266 3 VVIGGGIVGLSTAYELARRGLSVTLLERGDDpgSGASGRNAGLIHPGLRYLEPSELARLALEALD----LWEELEEELGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 83 DTGYNRVGAISLHTDEKKLDQMEERAYKRREDAPEigeiTRLSAEETKKLFPALSEEYSSVHISGAARVNGRLLRNALIS 162
Cdd:pfam01266 79 DCGFRRCGVLVLARDEEEEALEKLLAALRRLGVPA----ELLDAEELRELEPLLPGLRGGLFYPDGGHVDPARLLRALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 163 AAKKHGATFIKGDAVLVCEgnHINGVKVNDETILAEKVIVTAGAWAKEILNPlGINFLVTFQKGQIVHLQMENTATENMP 242
Cdd:pfam01266 155 AAEALGVRIIEGTEVTGIE--EEGGVWGVVTTGEADAVVNAAGAWADLLALP-GLRLPVRPVRGQVLVLEPLPEALLILP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 243 VVMPPNDQ---YILTFDNGHVVIGATHENDTGFDHRVTAGGLNEVFQKALTVAPGLenATMLETRVGFRPfTPGFLPVIG 319
Cdd:pfam01266 232 VPITVDPGrgvYLRPRADGRLLLGGTDEEDGFDDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLRP-LPDGLPIIG 308
|
330 340 350
....*....|....*....|....*....|..
gi 1033168231 320 PlPNFEGILVANGLGASGLTAGPYLGSELAKL 351
Cdd:pfam01266 309 R-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
5-367 |
3.43e-21 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 94.10 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQ-QVGQATDAA-AGIVCP-----------------WLSQRR----------- 54
Cdd:PRK00711 4 VVLGSGVIGVTSAWYLAQAGHEVTVIDRQpGPALETSFAnAGQISPgyaapwaapgvplkaikWLFQRHaplairpdgdp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 55 -------------NKAWYRIVKggAR-----YYS-SLIQQLEEdgETDTGYN--RVGAISLHTDEKKLDQMEER-AYKRR 112
Cdd:PRK00711 84 fqlrwmwqmlrncTASRYAVNK--SRmvrlaEYSrDCLKALRA--ETGIQYEgrQGGTLQLFRTQQQLDAAAKDiAVLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 113 EDAP-EIgeitrLSAEETKKLFPALSEeySSVHISGAARVNG------RLLRNALISAAKKHGATFIKGDAV--LVCEGN 183
Cdd:PRK00711 160 AGVPyEL-----LDRDELAAVEPALAG--VRHKLVGGLRLPNdetgdcQLFTQRLAAMAEQLGVKFRFNTPVdgLLVEGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 184 HINGVKVNDETILAEKVIVTAGAWAKEILNPLGINFLVTFQKGQIVHLQMENTATEnmPV--VMppnDQyilTFdngHVV 261
Cdd:PRK00711 233 RITGVQTGGGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTVPITDEDRA--PVstVL---DE---TY---KIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 262 IgathendTGFDHRVTAGGLNEV--FQKALTVA-------------PGLENATMLETRVGFRPFTPGFLPVIGPLPnFEG 326
Cdd:PRK00711 302 I-------TRFDDRIRVGGMAEIvgFDLRLDPArretlemvvrdlfPGGGDLSQATFWTGLRPMTPDGTPIVGATR-YKN 373
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1033168231 327 ILVANGLGASGLTAGPYLGSELAKLALGQSIELDLNDYDVA 367
Cdd:PRK00711 374 LWLNTGHGTLGWTMACGSGQLLADLISGRKPAIDADDLSVA 414
|
|
| solA |
PRK11259 |
N-methyl-L-tryptophan oxidase; |
5-361 |
1.78e-16 |
|
N-methyl-L-tryptophan oxidase;
Pssm-ID: 236887 [Multi-domain] Cd Length: 376 Bit Score: 79.88 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQQVGQATDAAAGIVcpwlsqrrnkawyRIVKG----GARYYSSLI--QQLEE 78
Cdd:PRK11259 7 IVIGLGSMGSAAGYYLARRGLRVLGLDRFMPPHQQGSSHGDT-------------RIIRHaygeGPAYVPLVLraQELWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 79 DGETDTG---YNRVGAISLHTDEKKLDQMEERAYKRREDAPEIgeitrLSAEETKKLFP--ALSEEYSSVHISGAARVNG 153
Cdd:PRK11259 74 ELERESGeplFVRTGVLNLGPADSDFLANSIRSARQHGLPHEV-----LDAAEIRRRFPqfRLPDGYIALFEPDGGFLRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 154 RLLRNALISAAKKHGATFIKGDAVLVCEgNHINGVKV--NDETILAEKVIVTAGAWAKEILNPLGINFLVTFQKGQIVHL 231
Cdd:PRK11259 149 ELAIKAHLRLAREAGAELLFNEPVTAIE-ADGDGVTVttADGTYEAKKLVVSAGAWVKDLLPPLELPLTPVRQVLAWFQA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 232 QMENTATENMPVvmppndqYILTFDNGHVVIGATHENDTGF-------DHRVTAgglNEVFQKALTVApglENATMLETR 304
Cdd:PRK11259 228 DGRYSEPNRFPA-------FIWEVPDGDQYYGFPAENGPGLkigkhngGQEITS---PDERDRFVTVA---EDGAELRPF 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033168231 305 VgfRPFTPGFLP-----------------VIGPLPNFEGILVANGLGASGLTAGPYLGSELAKLALGQSIELDL 361
Cdd:PRK11259 295 L--RNYLPGVGPclrgaactytntpdehfIIDTLPGHPNVLVASGCSGHGFKFASVLGEILADLAQDGTSDFDL 366
|
|
| LhgO |
COG0579 |
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism]; |
1-217 |
4.24e-16 |
|
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
Pssm-ID: 440344 [Multi-domain] Cd Length: 418 Bit Score: 79.03 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 1 MKSY--IVVGAGILGASTAYHLAKA-GANVTIVDRQ-QVGQ-ATDAAAGIVCPWL-----SQRRNKAwyriVKGGARYYs 70
Cdd:COG0579 2 MEMYdvVIIGAGIVGLALARELSRYeDLKVLVLEKEdDVAQeSSGNNSGVIHAGLyytpgSLKARLC----VEGNELFY- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 71 sliqQLEEdgETDTGYNRVGAISLHTDEKKLDQMEERaYKRREDAPeIGEITRLSAEETKKLFPALSEE-YSSVHISGAA 149
Cdd:COG0579 77 ----ELCR--ELGIPFKRCGKLVVATGEEEVAFLEKL-YERGKANG-VPGLEILDREELRELEPLLSDEgVAALYSPSTG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 150 RVNGRLLRNALISAAKKHGATFIKGDAV--LVCEGNHINgVKVNDETILAEKVIVTAGAWAKEILNPLGI 217
Cdd:COG0579 149 IVDPGALTRALAENAEANGVELLLNTEVtgIEREGDGWE-VTTNGGTIRARFVINAAGLYADRLAQMAGI 217
|
|
| MnmC_Cterm |
TIGR03197 |
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ... |
16-362 |
1.07e-15 |
|
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274478 [Multi-domain] Cd Length: 381 Bit Score: 77.69 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 16 TAYHLAKAGANVTIVDRQ-QVGQATDA-AAGIVCPWLSQRRNkAWYRIVKGGARYYSSLIQQLEEDGETdTGYNRVGAIS 93
Cdd:TIGR03197 1 TAYSLARRGWQVTLYEQDeAPAQGASGnPQGALYPLLSADDN-PLSRFFLAAFLYARRFYRQLAEAGFP-FDHEWCGVLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 94 LHTDEKKLDQMEERAykRREDAPEigEITR-LSAEETKKLFpALSEEYSSVHISGAARVNGRLLRNALISAAkkhgatfi 172
Cdd:TIGR03197 79 LAYDEKEAERLQKLL--EQLGFPE--ELARwVDAEQASQLA-GIPLPYGGLFFPQGGWLSPPQLCRALLAHA-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 173 kGDAVLVCEGNHINGVK----------VNDETILAEKVIVTAGAWAKEiLNPLGiNFLVTFQKGQIVHLQmENTATENMP 242
Cdd:TIGR03197 146 -GIRLTLHFNTEITSLErdgegwqlldANGEVIAASVVVLANGAQAPQ-LAQTA-HLPLRPVRGQVSHLP-ATEALSALK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 243 VVMPpNDQYILTFDNGHVVIGATHE---NDTGF---DHRvtagglnEVFQKALTVAPGLENATMLET-----RVGFRPFT 311
Cdd:TIGR03197 222 TVLC-YDGYLTPANNGEHCIGASYDrndDDLALreaDHA-------ENLERLAECLPALAWASEVDIsalqgRVGVRCAS 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033168231 312 PGFLPVIGPLPNFE-------------------------GILVANGLGASGLTAGPyLGSE-LAKLALGQSIELDLN 362
Cdd:TIGR03197 294 PDHLPLVGAVPDFEaikeayaelakdknrpiaepapyypGLYVLGGLGSRGLTSAP-LAAEiLAAQICGEPLPLERD 369
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
5-360 |
2.18e-14 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 74.50 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQQvGQATDAA---AGIVCPWLSQRRNKAwYRIVKGGARYYSSLIQQLEEDGE 81
Cdd:PRK01747 264 AIIGGGIAGAALALALARRGWQVTLYEADE-APAQGASgnrQGALYPLLSKDDNAL-SRFFRAAFLFARRFYDALPAAGV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 82 TdTGYNRVGAISLHTDEK---KLDQMEERaykrrEDAPEIgeITRLSAEETKKLFpALSEEYSSVHISGAARVNGRLLRN 158
Cdd:PRK01747 342 A-FDHDWCGVLQLAWDEKsaeKIAKMLAL-----GLPAEL--ARALDAEEAEELA-GLPVPCGGIFYPQGGWLCPAELCR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 159 ALISAAKKhGATFIKGDAV--LVCEGNHINgVKVNDETILAEKVIVTAGAwakeilnpLGINFLVTFQK-------GQIV 229
Cdd:PRK01747 413 ALLALAGQ-QLTIHFGHEVarLEREDDGWQ-LDFAGGTLASAPVVVLANG--------HDAARFAQTAHlplysvrGQVS 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 230 HLQmentATENMPVVMPP--NDQYIL-TFDNGHVVIGATHE---NDTGF---DHRVTAGGLNEVFQKALtvAPGLENATM 300
Cdd:PRK01747 483 HLP----TTPALSALKQVlcYDGYLTpQPANGTHCIGASYDrddTDTAFreaDHQENLERLAECLPQAL--WAKEVDVSA 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 301 LETRVGFRPFTPGFLPVIGPLPNFE----------------------GILVANGLGASGLTAGPYLGSELAKLALGQSIE 358
Cdd:PRK01747 557 LQGRVGFRCASRDRLPMVGNVPDEAatlaeyaalanqqpardaprlpGLYVAGALGSRGLCSAPLGAELLASQIEGEPLP 636
|
..
gi 1033168231 359 LD 360
Cdd:PRK01747 637 LE 638
|
|
| HpnW_proposed |
TIGR03364 |
FAD dependent oxidoreductase TIGR03364; This clade of FAD dependent oxidoreductases (members ... |
5-237 |
1.37e-10 |
|
FAD dependent oxidoreductase TIGR03364; This clade of FAD dependent oxidoreductases (members of the pfam01266 family) is syntenically associated with a family of proposed phosphonatase-like enzymes (TIGR03351) and is also found (less frequently) in association with phosphonate transporter components. A likely role for this enzyme involves the oxidative deamination of an aminophosphonate differring slightly from 2-aminoethylphosphonate, possibly 1-hydroxy-2-aminoethylphosphonate (see the comments for TIGR03351). Many members of the larger FAD dependent oxidoreductase family act as amino acid oxidative deaminases.
Pssm-ID: 132407 [Multi-domain] Cd Length: 365 Bit Score: 61.93 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQQvgQATDAAA---GIVCPwLSQRRNKAWYRIVKGGARYyssliqqLEEDGE 81
Cdd:TIGR03364 4 IIVGAGILGLAHAYAAARRGLSVTVIERSS--RAQGASVrnfGQVWP-TGQAPGPAWDRARRSREIW-------LELAAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 82 TDTGYNRVGAISLHTDEKKLDQMEERAYKRRedaPEIGEITRLSAEETKKLFPALSEEY--SSVHISGAARVNGRLLRNA 159
Cdd:TIGR03364 74 AGIWVRENGSLHLARTEEELAVLEEFAATRE---PAEYRVELLTPAEVAAKFPALRLDGlrGGLHSPDELRVEPREAIPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 160 LIS-AAKKHGATFIKGDAVlvcegNHINGVKVNDE--TILAEKVIVTAGA----WAKEILNPLGInflvtfqkgQIVHLQ 232
Cdd:TIGR03364 151 LAAyLAEQHGVEFHWNTAV-----TSVETGTVRTSrgDVHADQVFVCPGAdfetLFPELFAASGV---------RRCKLQ 216
|
....*
gi 1033168231 233 MENTA 237
Cdd:TIGR03364 217 MMRTA 221
|
|
| soxA_mon |
TIGR01377 |
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ... |
5-361 |
6.10e-10 |
|
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]
Pssm-ID: 130444 [Multi-domain] Cd Length: 380 Bit Score: 60.23 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQQVGQATDAAAGivcpwlSQRRNKAWYrivkgGARYYSSLI---QQLEEDGE 81
Cdd:TIGR01377 4 IVVGAGIMGCFAAYHLAKHGKKTLLLEQFDLPHSRGSSHG------QSRIIRKAY-----PEDFYTPMMlecYQLWAQLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 82 TDTGYNrvgaisLHTDEKKLD--QMEERAYKRREDAPEIGEITR--LSAEETKKLFP---------ALSEEYSSVHISGA 148
Cdd:TIGR01377 73 KEAGTK------LHRQTGLLLlgPKENQFLKTIQATLSRHGLEHelLSSKQLKQRFPnirvprnevGLLDPNGGVLYAEK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 149 ArvngrlLRnALISAAKKHGATFIKGDAVL---VCEGnhINGVKVNDETILAEKVIVTAGAWAKEILNPLGINFLVTFQK 225
Cdd:TIGR01377 147 A------LR-ALQELAEAHGATVRDGTKVVeiePTEL--LVTVKTTKGSYQANKLVVTAGAWTSKLLSPLGIEIPLQPLR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 226 GQIVHLQMENTATEN--------MPVVMPPNDQYILTFDNGHVVIGATH--------ENDTGF-DHRVTAGGLNEVFQKA 288
Cdd:TIGR01377 218 INVCYWREKEPGSYGvsqafpcfLVLGLNPHIYGLPSFEYPGLMKVYYHhgqqidpdERDCPFgADIEDVQILRKFVRDH 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033168231 289 LtvaPGLeNATMLETRVGFRPFTPGFLPVIGPLPNFEGILVANGLGASGLTAGPYLGSELAKLALGQSIELDL 361
Cdd:TIGR01377 298 L---PGL-NGEPKKGEVCMYTNTPDEHFVIDLHPKYDNVVIGAGFSGHGFKLAPVVGKILAELAMKLKPSYDL 366
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
1-33 |
1.70e-06 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 49.64 E-value: 1.70e-06
10 20 30
....*....|....*....|....*....|...
gi 1033168231 1 MKSYIVVGAGILGASTAYHLAKAGANVTIVDRQ 33
Cdd:PRK12409 1 MSHIAVIGAGITGVTTAYALAQRGYQVTVFDRH 33
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
1-36 |
9.72e-06 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 47.13 E-value: 9.72e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1033168231 1 MKSYIVVGAGILGASTAYHLAKAGANVTIVDRQ-QVG 36
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASdRVG 37
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
6-33 |
4.41e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.98 E-value: 4.41e-05
10 20
....*....|....*....|....*...
gi 1033168231 6 VVGAGILGASTAYHLAKAGANVTIVDRQ 33
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKR 28
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1-208 |
1.10e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.07 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 1 MKSYIVVGAGILGASTAYHLAKAGANVTIVDRQ-QVGQAT----------DAAAGIVCP---------------WLSQRR 54
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNdTPGGRArtferpgfrfDVGPSVLTMpgvlerlfrelgledYLELVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 55 NKAWYRIVKGG---ARYYSSL---IQQLE----EDGEtdtGYNRVGAISLHTDEKKLDQMEE------RAYKRREDAPEI 118
Cdd:COG1233 83 LDPAYRVPFPDgraLDLPRDLertAAELErlfpGDAE---AYRRFLAELRRLYDALLEDLLYrpllslRDLLRPLALARL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 119 GEITRLSA----------EETKKLF--------------PALseeYS----SVHISGAARVNG--RLLRNALISAAKKHG 168
Cdd:COG1233 160 LRLLLRSLrdllrryfkdPRLRALLagqalylglspdrtPAL---YAliayLEYAGGVWYPKGgmGALADALARLAEELG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1033168231 169 ATFIKGDAV--LVCEGNHINGVKVND-ETILAEKVIVTAGAWA 208
Cdd:COG1233 237 GEIRTGAEVerILVEGGRATGVRLADgEEIRADAVVSNADPAH 279
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
5-32 |
2.75e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 42.31 E-value: 2.75e-04
10 20
....*....|....*....|....*...
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDR 32
Cdd:TIGR02032 4 VVVGAGPAGASAAYRLADKGLRVLLLEK 31
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
6-34 |
6.32e-04 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 41.25 E-value: 6.32e-04
10 20
....*....|....*....|....*....
gi 1033168231 6 VVGAGILGASTAYHLAKAGANVTIVDRQQ 34
Cdd:COG1250 7 VIGAGTMGAGIAAVFANAGYEVVLLDISP 35
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
6-36 |
1.45e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 40.26 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|..
gi 1033168231 6 VVGAGILGASTAYHLAKAGANVTIVDR-QQVG 36
Cdd:PRK07233 4 IVGGGIAGLAAAYRLAKRGHEVTVFEAdDQLG 35
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
5-33 |
1.69e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 40.16 E-value: 1.69e-03
10 20
....*....|....*....|....*....
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQ 33
Cdd:COG3573 9 IVVGAGLAGLVAAAELADAGRRVLLLDQE 37
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
5-36 |
2.60e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 39.46 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|...
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDR-QQVG 36
Cdd:COG2072 10 VVIGAGQAGLAAAYHLRRAGIDFVVLEKaDDVG 42
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
5-36 |
2.78e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 39.52 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|...
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVD-RQQVG 36
Cdd:COG1231 11 VIVGAGLAGLAAARELRKAGLDVTVLEaRDRVG 43
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
5-226 |
2.95e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 39.19 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDR-QQVGQATDAAAGIVcpWLSQRRNKAWYRIVKgGARYYssLIQQLEEDGETD 83
Cdd:pfam00890 3 LVIGGGLAGLAAALAAAEAGLKVAVVEKgQPFGGATAWSSGGI--DALGNPPQGGIDSPE-LHPTD--TLKGLDELADHP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033168231 84 tgynrVGAISLHTDEKKLDQMEERA--YKRREDAPeigeiTRLSAeetkklFPALSEEYSSVHISGAAR---VNGRLLRN 158
Cdd:pfam00890 78 -----YVEAFVEAAPEAVDWLEALGvpFSRTEDGH-----LDLRP------LGGLSATWRTPHDAADRRrglGTGHALLA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033168231 159 ALISAAKKHGATFIKGDAV--LVCEGNHINGVKV------NDETILAEK-VIVTAGAWA--KEILNPLGINFLVTFQKG 226
Cdd:pfam00890 142 RLLEGLRKAGVDFQPRTAAddLIVEDGRVTGAVVenrrngREVRIRAIAaVLLATGGFGrlAELLLPAAGYADTTNPPA 220
|
|
| PRK08277 |
PRK08277 |
D-mannonate oxidoreductase; Provisional |
8-38 |
3.36e-03 |
|
D-mannonate oxidoreductase; Provisional
Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 38.73 E-value: 3.36e-03
10 20 30
....*....|....*....|....*....|..
gi 1033168231 8 GAGILGASTAYHLAKAGANVTIVDR-QQVGQA 38
Cdd:PRK08277 18 GGGVLGGAMAKELARAGAKVAILDRnQEKAEA 49
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
1-38 |
3.98e-03 |
|
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 38.68 E-value: 3.98e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1033168231 1 MKsYIVVGAGILGASTAYHLAKAGANVTIVDRQQVGQA 38
Cdd:COG1893 1 MK-IAILGAGAIGGLLGARLARAGHDVTLVARGAHAEA 37
|
|
| HSD10-like_SDR_c |
cd05371 |
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ... |
8-47 |
4.85e-03 |
|
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187629 [Multi-domain] Cd Length: 252 Bit Score: 38.04 E-value: 4.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1033168231 8 GAGILGASTAYHLAKAGANVTIVDRQQVGQATDAAAGIVC 47
Cdd:cd05371 10 GASGLGLATVERLLAQGAKVVILDLPNSPGETVAKLGDNC 49
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
2-35 |
5.41e-03 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 38.44 E-value: 5.41e-03
10 20 30
....*....|....*....|....*....|....*
gi 1033168231 2 KSYIVVGAGILGASTAYHLAKAG-ANVTIVDRQQV 35
Cdd:PRK07688 25 KHVLIIGAGALGTANAEMLVRAGvGKVTIVDRDYV 59
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
6-34 |
5.93e-03 |
|
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.
Pssm-ID: 426831 [Multi-domain] Cd Length: 147 Bit Score: 36.83 E-value: 5.93e-03
10 20
....*....|....*....|....*....
gi 1033168231 6 VVGAGILGASTAYHLAKAGANVTIVDRQQ 34
Cdd:pfam02558 3 ILGAGAIGSLLGARLAKAGHDVTLILRGA 31
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
5-53 |
8.80e-03 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 37.81 E-value: 8.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1033168231 5 IVVGAGILGASTAYHLAKAGANVTIVDRQQV---GQATDAAAGIVCPWLSQR 53
Cdd:COG1251 146 VVIGGGLIGLEAAAALRKRGLEVTVVERAPRllpRQLDEEAGALLQRLLEAL 197
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
4-32 |
9.01e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 37.59 E-value: 9.01e-03
10 20
....*....|....*....|....*....
gi 1033168231 4 YIVVGAGILGASTAYHLAKAGANVTIVDR 32
Cdd:pfam13738 158 VVVIGGYNSAVDAALELVRKGARVTVLYR 186
|
|
| |
