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Conserved domains on  [gi|2232797962|gb|UPS94679|]
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anaerobic glycerol-3-phosphate dehydrogenase subunit A [Escherichia coli]

Protein Classification

anaerobic glycerol-3-phosphate dehydrogenase subunit A( domain architecture ID 11485201)

anaerobic glycerol-3-phosphate dehydrogenase subunit A (GlpA) is part of the enzyme complex, composed of a catalytic dimer GlpA/B and a membrane-bound GlpC, that catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
25-536 0e+00

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


:

Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 1136.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTNGLFITLPEDDLSFQ 104
Cdd:PRK11101   23 RDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTDGLFITLPEDDLAFQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 105 ATFIRACEEAGISAEAIDPQQARIIEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGATV 184
Cdd:PRK11101  103 ATFIRACEEAGIEAEAIDPQQALILEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGDTV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 185 CGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILVPGDTIS 264
Cdd:PRK11101  183 CGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINNHVINRCRKPADADILVPGDTIS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 265 LIGTTSLRIDYNEIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYSGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 344
Cdd:PRK11101  263 LIGTTSTRIDYDQIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYAGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 345 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADLALPGSQEPAEVTLRKVISLPAPLRGSAVYRHGDRTPAWLS 424
Cdd:PRK11101  343 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADTPLPGSQEPAEVTLRKVISLPAPLRGSAVYRHGDRAPAWLS 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 425 EGRLHRSLVCECEAVTAGEVQYAVENLNVNSLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTSAQSIEQLSTFLNE 504
Cdd:PRK11101  423 EGRLDRSLVCECEAVTAGEVRYAVENLNVNNLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTPAQSIEQLSTFLNE 502
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2232797962 505 RWKGVQPIAWGDALRESEFTRWVYQGLCGLEK 536
Cdd:PRK11101  503 RWKGVQPIAWGDALRESEFTRWVYQGLCGLEP 534
 
Name Accession Description Interval E-value
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
25-536 0e+00

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 1136.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTNGLFITLPEDDLSFQ 104
Cdd:PRK11101   23 RDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTDGLFITLPEDDLAFQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 105 ATFIRACEEAGISAEAIDPQQARIIEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGATV 184
Cdd:PRK11101  103 ATFIRACEEAGIEAEAIDPQQALILEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGDTV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 185 CGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILVPGDTIS 264
Cdd:PRK11101  183 CGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINNHVINRCRKPADADILVPGDTIS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 265 LIGTTSLRIDYNEIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYSGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 344
Cdd:PRK11101  263 LIGTTSTRIDYDQIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYAGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 345 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADLALPGSQEPAEVTLRKVISLPAPLRGSAVYRHGDRTPAWLS 424
Cdd:PRK11101  343 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADTPLPGSQEPAEVTLRKVISLPAPLRGSAVYRHGDRAPAWLS 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 425 EGRLHRSLVCECEAVTAGEVQYAVENLNVNSLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTSAQSIEQLSTFLNE 504
Cdd:PRK11101  423 EGRLDRSLVCECEAVTAGEVRYAVENLNVNNLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTPAQSIEQLSTFLNE 502
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2232797962 505 RWKGVQPIAWGDALRESEFTRWVYQGLCGLEK 536
Cdd:PRK11101  503 RWKGVQPIAWGDALRESEFTRWVYQGLCGLEP 534
glycerol3P_GlpA TIGR03377
glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are ...
25-540 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are the A subunit, product of the glpA gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 274552 [Multi-domain]  Cd Length: 516  Bit Score: 955.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTNGLFITLPEDDLSFQ 104
Cdd:TIGR03377   2 RDLALRGLRCILLEQGDLAHGTTGRNHGLLHSGARYAVTDQESARECIEENRILKRIARHCVEDTGGLFITLPEDDLEFQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 105 ATFIRACEEAGISAEAIDPQQARIIEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGATV 184
Cdd:TIGR03377  82 KQFLAACREAGIPAEEIDPAEALRLEPNLNPDLIGAVKVPDGTVDPFRLVAANVLDAQEHGARIFTYTKVTGLIREGGRV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 185 CGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILVPGDTIS 264
Cdd:TIGR03377 162 TGVKVEDHKTGEEERIEAQVVINAAGIWAGRIAEYAGLDIRMFPAKGALLIMNHRINNTVINRCRKPSDADILVPGDTIS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 265 LIGTTSLRIDynEIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYSGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 344
Cdd:TIGR03377 242 IIGTTSERID--DPDDLPVTQEEVDVLLREGAKLAPMLAQTRILRAFAGVRPLVAVDDDPSGRNISRGIVLLDHAERDGL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 345 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADLALPGSQEPAEV-TLRKVISLPAPLRGSAVYRHGDRTPAWL 423
Cdd:TIGR03377 320 PGFITITGGKLTTYRLMAEWATDVVCKKLGNDRPCRTADEPLPGSEDPTAVkTLKKLISLPSPIAGSAVYRHGERAPQVL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 424 SEGRLHRSLVCECEAVTAGEVQYAVENLNVNSLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTSAQSIEQLSTFLN 503
Cdd:TIGR03377 400 KDNRLDNQVICECEMVTAGEVEYAIRELDVNNLVDLRRRTRLGMGTCQGEFCAYRAAGLLSREGLIDPEQSTELLREFLE 479
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 2232797962 504 ERWKGVQPIAWGDALRESEFTRWVYQGLCGLEKEQKD 540
Cdd:TIGR03377 480 ERWKGIRPILWGDALREAELTYWIYQGLFGLEHLPAD 516
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
25-485 3.85e-83

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440343 [Multi-domain]  Cd Length: 501  Bit Score: 267.38  E-value: 3.85e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARY------AVTdAESARECisenQILKRIARHCVEPtngLFITLP- 97
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYleqgefRLV-REALRER----EVLLRNAPHLVRP---LPFLLPl 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  98 EDDLSFQATFIRAceeaGISA-------------EAIDPQQARIIEPAVNP-ALIGAVKVPDGTVDPFRLTAANMLDAKE 163
Cdd:COG0578    73 YKGGERPAWLIRA----GLFLydllagrkglprhRRLSRAEALALAPLLRPdGLRGGFEYYDAQVDDARLVLELARTAAE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 164 HGAVILTAHEVTGLIREGATVCGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADL--RIRMFPAKGSLLIMDHR-- 239
Cdd:COG0578   149 RGAVVLNYTRVTGLLRDGGRVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPkaPRRVRPSKGSHLVVPRLfl 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 240 -INQHVInrCRKPSDADIL--VPGDTISLIGTTslRIDYNEIDDN-RVTAEEVDILLRE-----GEKLAPvmakTRILRA 310
Cdd:COG0578   229 pLDDALY--IFQNTDGRVVfaIPWEGRTLIGTT--DTDYDGDPDEpAATEEEIDYLLEAanryfARPLTR----DDVVST 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 311 YSGVRPLVASD-DDPSgrNVSRgivllDHAERDGLDGFITITGGKLMTYRLMAEWATDAVCRKLGNTR-PCTTADLALPG 388
Cdd:COG0578   301 YAGVRPLLDDGgKDTS--ALSR-----DHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRrPCWTADLPLPG 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 389 SQEPAEV---TLRKVISLPAPLRGSAVYRHGDRTPAWLSEGRLHRSL---VCECEAVTAGEVQYAVENLNVNSLLD-LRR 461
Cdd:COG0578   374 GDAGFDAfvaALAAAPGLPEALARRLLRRYGTRAEEVLALAAEDPDLgepLGPGLPYLEAEVVYAVRHEMARTLEDvLLR 453
                         490       500
                  ....*....|....*....|....*
gi 2232797962 462 RTRVGMGTCQGELCAC-RAAGLLQR 485
Cdd:COG0578   454 RTRLGLLDADAAAAAApAVAELMAA 478
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
25-359 5.99e-45

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: 161.80  E-value: 5.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERH-DIATGATGRNHGLLHSGARYAVTDAES--ARECISE-NQILKRIARHCVEPTNGLFITLPEDD 100
Cdd:pfam01266  16 YELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEPSELArlALEALDLwEELEEELGIDCGFRRCGVLVLARDEE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 101 LSFQATFIRACEEAGISAEAIDPQQARIIEPAVnPALIGAVKVPD-GTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIR 179
Cdd:pfam01266  96 EEALEKLLAALRRLGVPAELLDAEELRELEPLL-PGLRGGLFYPDgGHVDPARLLRALARAAEALGVRIIEGTEVTGIEE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 180 EGATVcGVHVrnhlTGETQAlhapvVVNAAGIWGQHIAEyADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILV- 258
Cdd:pfam01266 175 EGGVW-GVVT----TGEADA-----VVNAAGAWADLLAL-PGLRLPVRPVRGQVLVLEPLPEALLILPVPITVDPGRGVy 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 259 ---PGDTISLIGTTSlriDYNEIDDNRVTAEEVDILLREGEKLAPVMAktRILRAYSGVRPLvaSDDDPS-GRNVSRGIV 334
Cdd:pfam01266 244 lrpRADGRLLLGGTD---EEDGFDDPTPDPEEIEELLEAARRLFPALA--DIERAWAGLRPL--PDGLPIiGRPGSPGLY 316
                         330       340
                  ....*....|....*....|....*.
gi 2232797962 335 lldHAERDGLDGFITITG-GKLMTYR 359
Cdd:pfam01266 317 ---LATGHGGHGLTLAPGiGKLLAEL 339
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
432-485 3.43e-21

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381079 [Multi-domain]  Cd Length: 55  Bit Score: 86.82  E-value: 3.43e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2232797962 432 LVCECEAVTAGEVQYAVENLNVNSLLDLRRRTRVGMGTCQGELCACRAAGLLQR 485
Cdd:cd19946     2 IVCRCEEVTEGEIRDAIRRGAARDLDGLKRRTRAGMGRCQGRFCAPRVAELLAR 55
 
Name Accession Description Interval E-value
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
25-536 0e+00

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 1136.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTNGLFITLPEDDLSFQ 104
Cdd:PRK11101   23 RDCALRGLRCILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTDGLFITLPEDDLAFQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 105 ATFIRACEEAGISAEAIDPQQARIIEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGATV 184
Cdd:PRK11101  103 ATFIRACEEAGIEAEAIDPQQALILEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGDTV 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 185 CGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILVPGDTIS 264
Cdd:PRK11101  183 CGVRVRDHLTGETQEIHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINNHVINRCRKPADADILVPGDTIS 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 265 LIGTTSLRIDYNEIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYSGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 344
Cdd:PRK11101  263 LIGTTSTRIDYDQIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYAGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 345 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADLALPGSQEPAEVTLRKVISLPAPLRGSAVYRHGDRTPAWLS 424
Cdd:PRK11101  343 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADTPLPGSQEPAEVTLRKVISLPAPLRGSAVYRHGDRAPAWLS 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 425 EGRLHRSLVCECEAVTAGEVQYAVENLNVNSLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTSAQSIEQLSTFLNE 504
Cdd:PRK11101  423 EGRLDRSLVCECEAVTAGEVRYAVENLNVNNLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTPAQSIEQLSTFLNE 502
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2232797962 505 RWKGVQPIAWGDALRESEFTRWVYQGLCGLEK 536
Cdd:PRK11101  503 RWKGVQPIAWGDALRESEFTRWVYQGLCGLEP 534
glycerol3P_GlpA TIGR03377
glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are ...
25-540 0e+00

glycerol-3-phosphate dehydrogenase, anaerobic, A subunit; Members of this protein family are the A subunit, product of the glpA gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]


Pssm-ID: 274552 [Multi-domain]  Cd Length: 516  Bit Score: 955.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARYAVTDAESARECISENQILKRIARHCVEPTNGLFITLPEDDLSFQ 104
Cdd:TIGR03377   2 RDLALRGLRCILLEQGDLAHGTTGRNHGLLHSGARYAVTDQESARECIEENRILKRIARHCVEDTGGLFITLPEDDLEFQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 105 ATFIRACEEAGISAEAIDPQQARIIEPAVNPALIGAVKVPDGTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGATV 184
Cdd:TIGR03377  82 KQFLAACREAGIPAEEIDPAEALRLEPNLNPDLIGAVKVPDGTVDPFRLVAANVLDAQEHGARIFTYTKVTGLIREGGRV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 185 CGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILVPGDTIS 264
Cdd:TIGR03377 162 TGVKVEDHKTGEEERIEAQVVINAAGIWAGRIAEYAGLDIRMFPAKGALLIMNHRINNTVINRCRKPSDADILVPGDTIS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 265 LIGTTSLRIDynEIDDNRVTAEEVDILLREGEKLAPVMAKTRILRAYSGVRPLVASDDDPSGRNVSRGIVLLDHAERDGL 344
Cdd:TIGR03377 242 IIGTTSERID--DPDDLPVTQEEVDVLLREGAKLAPMLAQTRILRAFAGVRPLVAVDDDPSGRNISRGIVLLDHAERDGL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 345 DGFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADLALPGSQEPAEV-TLRKVISLPAPLRGSAVYRHGDRTPAWL 423
Cdd:TIGR03377 320 PGFITITGGKLTTYRLMAEWATDVVCKKLGNDRPCRTADEPLPGSEDPTAVkTLKKLISLPSPIAGSAVYRHGERAPQVL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 424 SEGRLHRSLVCECEAVTAGEVQYAVENLNVNSLLDLRRRTRVGMGTCQGELCACRAAGLLQRFNVTTSAQSIEQLSTFLN 503
Cdd:TIGR03377 400 KDNRLDNQVICECEMVTAGEVEYAIRELDVNNLVDLRRRTRLGMGTCQGEFCAYRAAGLLSREGLIDPEQSTELLREFLE 479
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 2232797962 504 ERWKGVQPIAWGDALRESEFTRWVYQGLCGLEKEQKD 540
Cdd:TIGR03377 480 ERWKGIRPILWGDALREAELTYWIYQGLFGLEHLPAD 516
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
25-485 3.85e-83

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440343 [Multi-domain]  Cd Length: 501  Bit Score: 267.38  E-value: 3.85e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARY------AVTdAESARECisenQILKRIARHCVEPtngLFITLP- 97
Cdd:COG0578     1 RDAAGRGLSVALVEKGDFASGTSSRSSKLIHGGLRYleqgefRLV-REALRER----EVLLRNAPHLVRP---LPFLLPl 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  98 EDDLSFQATFIRAceeaGISA-------------EAIDPQQARIIEPAVNP-ALIGAVKVPDGTVDPFRLTAANMLDAKE 163
Cdd:COG0578    73 YKGGERPAWLIRA----GLFLydllagrkglprhRRLSRAEALALAPLLRPdGLRGGFEYYDAQVDDARLVLELARTAAE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 164 HGAVILTAHEVTGLIREGATVCGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADL--RIRMFPAKGSLLIMDHR-- 239
Cdd:COG0578   149 RGAVVLNYTRVTGLLRDGGRVWGVTVRDRLTGEEFTVRARVVVNATGPWVDELRALDGPkaPRRVRPSKGSHLVVPRLfl 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 240 -INQHVInrCRKPSDADIL--VPGDTISLIGTTslRIDYNEIDDN-RVTAEEVDILLRE-----GEKLAPvmakTRILRA 310
Cdd:COG0578   229 pLDDALY--IFQNTDGRVVfaIPWEGRTLIGTT--DTDYDGDPDEpAATEEEIDYLLEAanryfARPLTR----DDVVST 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 311 YSGVRPLVASD-DDPSgrNVSRgivllDHAERDGLDGFITITGGKLMTYRLMAEWATDAVCRKLGNTR-PCTTADLALPG 388
Cdd:COG0578   301 YAGVRPLLDDGgKDTS--ALSR-----DHVIEVGPAGLLSIAGGKLTTYRKMAEDAVDAAARLLGLPRrPCWTADLPLPG 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 389 SQEPAEV---TLRKVISLPAPLRGSAVYRHGDRTPAWLSEGRLHRSL---VCECEAVTAGEVQYAVENLNVNSLLD-LRR 461
Cdd:COG0578   374 GDAGFDAfvaALAAAPGLPEALARRLLRRYGTRAEEVLALAAEDPDLgepLGPGLPYLEAEVVYAVRHEMARTLEDvLLR 453
                         490       500
                  ....*....|....*....|....*
gi 2232797962 462 RTRVGMGTCQGELCAC-RAAGLLQR 485
Cdd:COG0578   454 RTRLGLLDADAAAAAApAVAELMAA 478
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
25-359 5.99e-45

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: 161.80  E-value: 5.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERH-DIATGATGRNHGLLHSGARYAVTDAES--ARECISE-NQILKRIARHCVEPTNGLFITLPEDD 100
Cdd:pfam01266  16 YELARRGLSVTLLERGdDPGSGASGRNAGLIHPGLRYLEPSELArlALEALDLwEELEEELGIDCGFRRCGVLVLARDEE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 101 LSFQATFIRACEEAGISAEAIDPQQARIIEPAVnPALIGAVKVPD-GTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIR 179
Cdd:pfam01266  96 EEALEKLLAALRRLGVPAELLDAEELRELEPLL-PGLRGGLFYPDgGHVDPARLLRALARAAEALGVRIIEGTEVTGIEE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 180 EGATVcGVHVrnhlTGETQAlhapvVVNAAGIWGQHIAEyADLRIRMFPAKGSLLIMDHRINQHVINRCRKPSDADILV- 258
Cdd:pfam01266 175 EGGVW-GVVT----TGEADA-----VVNAAGAWADLLAL-PGLRLPVRPVRGQVLVLEPLPEALLILPVPITVDPGRGVy 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 259 ---PGDTISLIGTTSlriDYNEIDDNRVTAEEVDILLREGEKLAPVMAktRILRAYSGVRPLvaSDDDPS-GRNVSRGIV 334
Cdd:pfam01266 244 lrpRADGRLLLGGTD---EEDGFDDPTPDPEEIEELLEAARRLFPALA--DIERAWAGLRPL--PDGLPIiGRPGSPGLY 316
                         330       340
                  ....*....|....*....|....*.
gi 2232797962 335 lldHAERDGLDGFITITG-GKLMTYR 359
Cdd:pfam01266 317 ---LATGHGGHGLTLAPGiGKLLAEL 339
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
27-316 2.17e-35

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 136.19  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  27 CAL----RGLRVILVERHDIATGATGRNHGLLHSGARYAVTDA-----ESARECISEnqILKRIARHC-VEPTNGLFITL 96
Cdd:COG0665    17 TAYhlarRGLDVTVLERGRPGSGASGRNAGQLRPGLAALADRAlvrlaREALDLWRE--LAAELGIDCdFRRTGVLYLAR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  97 PEDDLSFQATFIRACEEAGISAEAIDPQQARIIEPAVN-PALIGAVKVP-DGTVDPFRLTAANMLDAKEHGAVILTAHEV 174
Cdd:COG0665    95 TEAELAALRAEAEALRALGLPVELLDAAELREREPGLGsPDYAGGLYDPdDGHVDPAKLVRALARAARAAGVRIREGTPV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 175 TGLIREGATVCGVHVrnhltgETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKGSLLI---MDHRINQHVInrcrkp 251
Cdd:COG0665   175 TGLEREGGRVTGVRT------ERGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVtepLPDLPLRPVL------ 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2232797962 252 SDADI---LVPGDTIsLIGTTSlriDYNEIDDnRVTAEEVDILLREGEKLAPVMAKTRILRAYSGVRP 316
Cdd:COG0665   243 DDTGVylrPTADGRL-LVGGTA---EPAGFDR-APTPERLEALLRRLRRLFPALADAEIVRAWAGLRP 305
PLN02464 PLN02464
glycerol-3-phosphate dehydrogenase
26-391 8.18e-35

glycerol-3-phosphate dehydrogenase


Pssm-ID: 215257 [Multi-domain]  Cd Length: 627  Bit Score: 138.76  E-value: 8.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  26 DCALRGLRVILVERHDIATGATGRNHGLLHSGARY---AVTDAESAR-----ECISENQILKRIARH------CVEPTNG 91
Cdd:PLN02464   89 DAATRGLRVGLVEREDFSSGTSSRSTKLIHGGVRYlekAVFQLDYGQlklvfHALEERKQLIENAPHlchalpIMTPCYD 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  92 LFiTLPEDDLSFQATFIRACEEAGISAEAIDPQQARIIEPAVNP-----ALIGAVKVPDGTVDPFRLTAANMLDAKEHGA 166
Cdd:PLN02464  169 WF-EVPYYWAGLKAYDLVAGPRLLHLSRYYSAKESLELFPTLAKkgkdgSLKGTVVYYDGQMNDSRLNVALACTAALAGA 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 167 VILTAHEVTGLIREGAT--VCGVHVRNHLTGETQALHAPVVVNAAGIWGQHIAEYADLRIR--MFPAKGSLLIM-DHRIn 241
Cdd:PLN02464  248 AVLNYAEVVSLIKDESTgrIVGARVRDNLTGKEFDVYAKVVVNAAGPFCDEVRKMADGKAKpmICPSSGVHIVLpDYYS- 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 242 qhvinrcrkPSDADILVP--------------GDTIslIGTTSLRIDYNEIDdnRVTAEEVDILLREGEKLAPVMAK-TR 306
Cdd:PLN02464  327 ---------PEGMGLIVPktkdgrvvfmlpwlGRTV--AGTTDSKTPITMLP--EPHEDEIQFILDAISDYLNVKVRrSD 393
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 307 ILRAYSGVRPLVAsddDPSGR---NVSRgivllDHAERDGLDGFITITGGKLMTYRLMAEWATDAVCR--KLGNTRPCTT 381
Cdd:PLN02464  394 VLSAWSGIRPLAV---DPSAKsteSISR-----DHVVCEEPDGLVTITGGKWTTYRSMAEDAVDAAIKsgKLSPTNGCVT 465
                         410
                  ....*....|
gi 2232797962 382 ADLALPGSQE 391
Cdd:PLN02464  466 TDLPLVGAEG 475
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
25-467 4.32e-32

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 129.32  E-value: 4.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARY-------AVtdaesaRECISENQILKRIARHCVEPTNglFItLP 97
Cdd:PRK13369   23 RDAAGRGLKVLLCEKDDLAQGTSSRSGKLVHGGLRYleyyefrLV------REALIEREVLLAAAPHIIWPMR--FV-LP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  98 EDDLSFQATFIRAceeaGI-------------SAEAIDPQQARIIEPaVNPALIGAVKVPDGTVDPFRLTAANMLDAKEH 164
Cdd:PRK13369   94 HSPEDRPAWLVRL----GLflydhlggrkrlpGTRTLDLRRDPEGAP-LKPEYTKGFEYSDCWVDDARLVVLNALDAAER 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 165 GAVILTAHEVTGLIREGATvCGVHVRNHlTGETQALHAPVVVNAAGIWgqhIAEYADLRIRMFPAKGSLLImdhRINQHV 244
Cdd:PRK13369  169 GATILTRTRCVSARREGGL-WRVETRDA-DGETRTVRARALVNAAGPW---VTDVIHRVAGSNSSRNVRLV---KGSHIV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 245 INRCRKPSDADILVPGD-----------TISLIGTTSlrIDYN-EIDDNRVTAEEVDILLREG-----EKLAPvmakTRI 307
Cdd:PRK13369  241 VPKFWDGAQAYLFQNPDkrvifanpyegDFTLIGTTD--IAYEgDPEDVAADEEEIDYLLDAAnryfkEKLRR----EDV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 308 LRAYSGVRPLVasdDDPSGR--NVSRGIVLLDHAERDGLDgFITITGGKLMTYRLMAEWATDAVCRKLGNTRPCTTADLA 385
Cdd:PRK13369  315 VHSFSGVRPLF---DDGAGNpsAVTRDYVFDLDAETGGAP-LLSVFGGKITTFRKLAEHALERLKPFFPQMGGDWTAGAP 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 386 LPGSQEPAEVTLRKVIS-------LPAPLRGSAVYRHGDRTPAWLSEGRLHRSL-VCECEAVTAGEVQYAVENLNVNSLL 457
Cdd:PRK13369  391 LPGGDIANADFDTFADDlrdrypwLPRPLAHRYARLYGTRAKDVLGGARSLEDLgRHFGGGLTEAEVRYLVAREWARTAE 470
                         490
                  ....*....|.
gi 2232797962 458 D-LRRRTRVGM 467
Cdd:PRK13369  471 DiLWRRTKLGL 481
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
25-467 7.83e-29

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 119.86  E-value: 7.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  25 RDCALRGLRVILVERHDIATGATGRNHGLLHSGARYA-------VtdaesaRECISENQILKRIARHCVEPTN------- 90
Cdd:PRK12266   23 RDAAGRGLSVLLCEQDDLASATSSASTKLIHGGLRYLehyefrlV------REALAEREVLLRMAPHIIWPMRfvlphrp 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  91 ----------GLFI--------TLPeddlsfqATfiraceeagisaeaidpqqaRIIEPAVNPAliGAVKVP-------- 144
Cdd:PRK12266   97 hlrpawmiraGLFLydhlgkrkSLP-------GS--------------------RGLDLGRDPA--GSPLKPeitrgfey 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 145 -DGTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGAtVCGVHVRNHLTGETQALHAPVVVNAAGIW-GQHIAEYADL 222
Cdd:PRK12266  148 sDCWVDDARLVVLNARDAAERGAEILTRTRVVSARRENG-LWHVTLEDTATGKRYTVRARALVNAAGPWvKQFLDDGLGL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 223 ----RIRMfpAKGSLLIMdHRINQHvinrcrkpSDADILVPGD-----TI------SLIGTTSlrIDYN-EIDDNRVTAE 286
Cdd:PRK12266  227 pspyGIRL--VKGSHIVV-PRLFDH--------DQAYILQNPDgrivfAIpyeddfTLIGTTD--VEYKgDPAKVAISEE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 287 EVDILLregeKLAPVMAKTRILRA-----YSGVRPLVasdDDPSGRN--VSRGIVLLDHAERDG--LdgfITITGGKLMT 357
Cdd:PRK12266  294 EIDYLC----KVVNRYFKKQLTPAdvvwtYSGVRPLC---DDESDSAqaITRDYTLELDDENGGapL---LSVFGGKITT 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 358 YRLMAEWATDAVCRKLGNTRPCTTADLALPG------SQEPAEVTLRKVIS-LPAPLRGSAVYRHGDRTPAWLSEGrlhR 430
Cdd:PRK12266  364 YRKLAEHALEKLAPYLPQMGPAWTAGAPLPGgdfpgdRFDALAAALRRRYPwLPEALARRLARAYGTRAERLLGGA---T 440
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 2232797962 431 SLVCECEAVTAG----EVQYAVENLNVNSLLD-LRRRTRVGM 467
Cdd:PRK12266  441 SLADLGEHFGHGlyeaEVDYLVEHEWARTAEDiLWRRTKLGL 482
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
29-247 1.55e-27

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 114.86  E-value: 1.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  29 LRGLRVILVER-HDIATGATGRNHGLLHSGArYAVTDAESARECISENQILKRIAR-HCV--EPTNGLFITLPEDDLSFQ 104
Cdd:COG0579    26 YEDLKVLVLEKeDDVAQESSGNNSGVIHAGL-YYTPGSLKARLCVEGNELFYELCReLGIpfKRCGKLVVATGEEEVAFL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 105 ATFIRACEEAGISA-EAIDPQQARIIEPAVNPALIGAVKVPDGT-VDPFRLTAANMLDAKEHGAVILTAHEVTGLIREGA 182
Cdd:COG0579   105 EKLYERGKANGVPGlEILDREELRELEPLLSDEGVAALYSPSTGiVDPGALTRALAENAEANGVELLLNTEVTGIEREGD 184
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2232797962 183 tvcGVHVRnhlTGeTQALHAPVVVNAAGIWGQHIAEYA--DLRIRMFPAKGSLLIMDHRinQHVINR 247
Cdd:COG0579   185 ---GWEVT---TN-GGTIRARFVINAAGLYADRLAQMAgiGKDFGIFPVKGEYLVLDKP--AELVNA 242
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
432-485 3.43e-21

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381079 [Multi-domain]  Cd Length: 55  Bit Score: 86.82  E-value: 3.43e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2232797962 432 LVCECEAVTAGEVQYAVENLNVNSLLDLRRRTRVGMGTCQGELCACRAAGLLQR 485
Cdd:cd19946     2 IVCRCEEVTEGEIRDAIRRGAARDLDGLKRRTRAGMGRCQGRFCAPRVAELLAR 55
Fer2_BFD-like cd19942
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ...
431-482 6.31e-09

[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.


Pssm-ID: 381075 [Multi-domain]  Cd Length: 49  Bit Score: 52.06  E-value: 6.31e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2232797962 431 SLVCECEAVTAGEVQYAVENLNvNSLLDLRRRTRVGMGTCQgeLCACRAAGL 482
Cdd:cd19942     1 ALVCECFAVTEKELREAIRKGG-LKTVEELLTGTGAGGGCG--VCHPHVAQL 49
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
31-240 1.37e-08

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 57.14  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962  31 GLRVILVER-HDIATGATGRNHGLLHSG---------ARYAVTDAESARECISENQIlkriaRHcvEPTNGLFITLPEDD 100
Cdd:PRK11728   27 GARIAVLEKeSGPARHQTGHNSGVIHAGvyytpgslkARFCRRGNEATKAFCDQHGI-----PY--EECGKLLVATSELE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 101 LSFQATFIRACEEAGISAEAIDPQQARIIEPAVNPalIGAVKVPD-GTVDPFRLTAANMLDAKEHGAVILTAHEVTGLIR 179
Cdd:PRK11728  100 LERMEALYERARANGIEVERLDAEELREREPNIRG--LGAIFVPStGIVDYRAVAEAMAELIQARGGEIRLGAEVTALDE 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2232797962 180 EGATVcgvhvrnHLTGETQALHAPVVVNAAGIwgqhiaeYADLRIRMFPAKGsllimDHRI 240
Cdd:PRK11728  178 HANGV-------VVRTTQGEYEARTLINCAGL-------MSDRLAKMAGLEP-----DFRI 219
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
432-485 2.93e-05

BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).


Pssm-ID: 461261 [Multi-domain]  Cd Length: 50  Bit Score: 41.36  E-value: 2.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2232797962 432 LVCECEAVTAGEVQYAVENlNVNSLLDLRRRTRVGMGtCQGelCACRAAGLLQR 485
Cdd:pfam04324   1 IVCRCFGVTDGEIRDAIRE-GLTTVEEVKRRTKAGTG-CGS--CRPAIEEILAE 50
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
161-241 8.23e-05

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 45.21  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 161 AKEHGAVILTAHEVTGLIREGATVCGVHVRNHlTGETQALHAPVVVNAAGIWGqHIAEyadLRIRMFPAKGSLLIMDHRI 240
Cdd:COG1053   144 ALRLGVEIFTETEVLDLIVDDGRVVGVVARDR-TGEIVRIRAKAVVLATGGFG-RNYE---MRAEYLPEAEGALSTNAPG 218

                  .
gi 2232797962 241 N 241
Cdd:COG1053   219 N 219
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
161-212 4.52e-04

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 42.91  E-value: 4.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2232797962 161 AKEHGAVILTAHEVTGLIREGATVCGVHVRNhltGETqaLHAPVVVNAAGIW 212
Cdd:COG1233   232 AEELGGEIRTGAEVERILVEGGRATGVRLAD---GEE--IRADAVVSNADPA 278
PRK00711 PRK00711
D-amino acid dehydrogenase;
108-235 9.29e-04

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 41.71  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232797962 108 IRACEEAGISAEAIDPQQARIIEPA---VNPALIGAVKVP-DGTVDPFRLTA--ANMldAKEHGAVILTAHEVTGLIREG 181
Cdd:PRK00711  154 IAVLEEAGVPYELLDRDELAAVEPAlagVRHKLVGGLRLPnDETGDCQLFTQrlAAM--AEQLGVKFRFNTPVDGLLVEG 231
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2232797962 182 ATVCGVHVrnhltgETQALHAPVVVNAAGIWGQHIAEYADLRIRMFPAKG-SLLI 235
Cdd:PRK00711  232 GRITGVQT------GGGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGySLTV 280
PRK06185 PRK06185
FAD-dependent oxidoreductase;
168-210 1.50e-03

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 41.00  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2232797962 168 ILTAHEVTGLIREGATVCGVHVRNhlTGETQALHAPVVVNAAG 210
Cdd:PRK06185  126 LRMGAEVTGLIEEGGRVTGVRART--PDGPGEIRADLVVGADG 166
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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