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Conserved domains on  [gi|616690648|gb|KAE88217|]
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dehydrosqualene desaturase [Staphylococcus aureus VET0402R]

Protein Classification

phytoene desaturase family protein( domain architecture ID 11440907)

phytoene desaturase family protein is an NAD(P)/FAD-dependent oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to phytoene desaturase, which converts phytoene into 3,4-didehydrolycopene via several intermediates by introducing up to five double bonds into phytoene

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0009055|GO:0016117|GO:0016116
SCOP:  4000128|3000055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-501 8.63e-161

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


:

Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 465.09  E-value: 8.63e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVMMPDVYKDVFTMCGEnyEDYIELR 80
Cdd:COG1233    4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLTMPGVLERLFRELGL--EDYLELV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  81 QLRYIYDVYFDRDDRITVPTDLAELQHMLESIEPGSTHGFMSFLTDVYKKYEIARRYFLERTYRKPSDFYNMTSLVQGAK 160
Cdd:COG1233   82 PLDPAYRVPFPDGRALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLYRPLLSLRDLLRPLALARLLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 161 LKTLNhADQLIEHYIDNEKIQKLLAFQTLYIGIDPKRGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQLNKDLGVNIE 240
Cdd:COG1233  162 LLLRS-LRDLLRRYFKDPRLRALLAGQALYLGLSPDRTPALYALIAYLEYAGGVWYPKGGMGALADALARLAEELGGEIR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 241 LNAEIEQIIIDPKfkRADAIKV-NGDIRKFDKILCTADFPSVAESLMPDFAPIKKYPpHKIADLDYSCSAFLMYIGIDID 319
Cdd:COG1233  241 TGAEVERILVEGG--RATGVRLaDGEEIRADAVVSNADPAHTYLRLLGEEALPARYR-RRLERFRYSPSAFKLYLGLDGP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 320 VtDQVRLHNVIFSDDFRGNIEEIFEGRLSYDPSIYVYVPAVADKSLAPEGKTGIYVLMPTPelkTGSGIDWsdEALTQQI 399
Cdd:COG1233  318 L-PGLAHHTIHLSEDYEAAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVPVP---YGLEDAW--DELKEEY 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 400 KEIIYRKLAtiEVFEDIKSHIVSETIFTPNDFEQTYHAKFGSAFGLMPTLAQSNYYRPQNVSRDYKDLYFAGASTHPGAG 479
Cdd:COG1233  392 AERILARLE--RYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRPSNYRTPIPGLYLVGASTHPGGG 469

                        490       500
                 ....*....|....*....|..
gi 616690648 480 VPIVLTSAKITVDEMIKDIEQG 501
Cdd:COG1233  470 VPGVLISGRLAARRILKDLKRA 491
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-501 8.63e-161

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 465.09  E-value: 8.63e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVMMPDVYKDVFTMCGEnyEDYIELR 80
Cdd:COG1233    4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLTMPGVLERLFRELGL--EDYLELV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  81 QLRYIYDVYFDRDDRITVPTDLAELQHMLESIEPGSTHGFMSFLTDVYKKYEIARRYFLERTYRKPSDFYNMTSLVQGAK 160
Cdd:COG1233   82 PLDPAYRVPFPDGRALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLYRPLLSLRDLLRPLALARLLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 161 LKTLNhADQLIEHYIDNEKIQKLLAFQTLYIGIDPKRGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQLNKDLGVNIE 240
Cdd:COG1233  162 LLLRS-LRDLLRRYFKDPRLRALLAGQALYLGLSPDRTPALYALIAYLEYAGGVWYPKGGMGALADALARLAEELGGEIR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 241 LNAEIEQIIIDPKfkRADAIKV-NGDIRKFDKILCTADFPSVAESLMPDFAPIKKYPpHKIADLDYSCSAFLMYIGIDID 319
Cdd:COG1233  241 TGAEVERILVEGG--RATGVRLaDGEEIRADAVVSNADPAHTYLRLLGEEALPARYR-RRLERFRYSPSAFKLYLGLDGP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 320 VtDQVRLHNVIFSDDFRGNIEEIFEGRLSYDPSIYVYVPAVADKSLAPEGKTGIYVLMPTPelkTGSGIDWsdEALTQQI 399
Cdd:COG1233  318 L-PGLAHHTIHLSEDYEAAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVPVP---YGLEDAW--DELKEEY 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 400 KEIIYRKLAtiEVFEDIKSHIVSETIFTPNDFEQTYHAKFGSAFGLMPTLAQSNYYRPQNVSRDYKDLYFAGASTHPGAG 479
Cdd:COG1233  392 AERILARLE--RYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRPSNYRTPIPGLYLVGASTHPGGG 469

                        490       500
                 ....*....|....*....|..
gi 616690648 480 VPIVLTSAKITVDEMIKDIEQG 501
Cdd:COG1233  470 VPGVLISGRLAARRILKDLKRA 491
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 5-497 8.18e-134

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 396.65  E-value: 8.18e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648    5 VIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVMMPDVYKDVFTMCGENYEDYIELRQLRY 84
Cdd:TIGR02734   3 VIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVITMPEALEELFALAGRDLADYVELVPLDP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   85 IYDVYFDRDDRITVPTDLAELQHMLESIEPGSTHGFMSFLTDVYKKYEIARRYFLERTYRKPSDFYNmTSLVQGAKLKTL 164
Cdd:TIGR02734  83 FYRLCWEDGSQLDVDNDQEELEAQIARFNPGDVAGYRRFLDYAERVYREGYRKLGYVPFLSPRDLLR-ADAPQLLALLAW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  165 NHADQLIEHYIDNEKIQKLLAFQTLYIGIDPKRGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQLNKDLGVNIELNAE 244
Cdd:TIGR02734 162 RSLYSKVARFFSDERLRQAFSFHALFLGGNPFRTPSIYALISALEREWGVWFPRGGTGALVAAMAKLAEDLGGELRLNAE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  245 IEQiiIDPKFKRADAIkVNGDIRKF--DKILCTADFPSVAESLMPDfAPIKKYPPHKIADLDYSCSAFLMYIGIDID--V 320
Cdd:TIGR02734 242 VIR--IETEGGRATAV-HLADGERLdaDAVVSNADLHHTYRRLLPN-HPRRRYPAARLSRKRPSPSLFVLYFGLLGVdgH 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  321 TDQVRLHNVIFSDDFRGNIEEIFE-GRLSYDPSIYVYVPAVADKSLAPEGKTGIYVLMPTPELKTGsGIDWSDEAltQQI 399
Cdd:TIGR02734 318 WPQLAHHTLCFGPRYKELFDEIFRkGRLAEDPSLYLHRPTVTDPSLAPPGCESLYVLAPVPHLGTA-DVDWSVEG--PRY 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  400 KEIIYRKLATIEVfEDIKSHIVSETIFTPNDFEQTYHAKFGSAFGLMPTLAQSNYYRPQNVSRDYKDLYFAGASTHPGAG 479
Cdd:TIGR02734 395 RDRILAYLEERAI-PGLRDRIVVERTFTPADFRDRYNAWLGSAFSLEHTLTQSAWFRPHNRDRKIDNLYLVGAGTHPGAG 473

                         490
                  ....*....|....*...
gi 616690648  480 VPIVLTSAKITVDEMIKD 497
Cdd:TIGR02734 474 VPGVLGSAKATAKLMLGD 491
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 10-495 2.58e-26

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 111.04  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   10 VTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVmmPDVYKDVFTMCGE-NYEDYIELRQLRYIYDV 88
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF--HGAQPPLLALLKElGLEDRLVLPDPAPFYTV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   89 YFDRDDRitVPTDLAELQHMLEsiepgsthGFMSFLTDVYKKyEIARRYFLERTYRKPSDFYNMTSLVQGAKLKTLNH-- 166
Cdd:pfam01593  79 LFAGGRR--YPGDFRRVPAGWE--------GLLEFGRLLSIP-EKLRLGLAALASDALDEFDLDDFSLAESLLFLGRRgp 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  167 -ADQLIEHYIDNEKIQKLLAFQTLYIGIDPK--RGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQlnKDLGVNIELNA 243
Cdd:pfam01593 148 gDVEVWDRLIDPELFAALPFASGAFAGDPSElsAGLALPLLWALLGEGGSLLLPRGGLGALPDALAA--QLLGGDVRLNT 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  244 EIEQIIidpkfKRADAIKV---NGDIRKFDKILCTADfPSVAESLMPDfAPIKKYPPHKIADLDY--SCSAFLMYigidi 318
Cdd:pfam01593 226 RVRSID-----REGDGVTVtltDGEVIEADAVIVTVP-LGVLKRILFT-PPLPPEKARAIRNLGYgpVNKVHLEF----- 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  319 dvtDQVRLHNvifsDDFRGNIEEIFEGRlsydPSIYVYVPavaDKSLAPEGKTGIYVLMptpelkTGSGiDW-------S 391
Cdd:pfam01593 294 ---DRKFWPD----LGLLGLLSELLTGL----GTAFSWLT---FPNRAPPGKGLLLLVY------VGPG-DRareleglS 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  392 DEALTQQIKEIIyRKLATIEVFEDIKSHIVSetiFTPNDFeqtyhakFGSAFGLMPTLAQSNYYRPQNVSRDyKDLYFAG 471
Cdd:pfam01593 353 DEELLQAVLRDL-RKLFGEEAPEPLRVLVSD---WHTDPW-------PRGSYSLPQYGPGHDDYRPLARTPD-PGLFFAG 420

                         490       500
                  ....*....|....*....|....*.
gi 616690648  472 ASTHPG--AGVPIVLTSAKITVDEMI 495
Cdd:pfam01593 421 EHTSTGypGTVEGAIESGRRAARAVL 446
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 1-53 4.17e-11

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 64.87  E-value: 4.17e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQG--HEVTIFEKNTNVGGRMNQLKKDGFTFDMGP 53
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKDGFPIELGP 55
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-49 1.48e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 42.11  E-value: 1.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 616690648     2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNV--------GGRMNQLKKDGFTF 49
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARlrqlesllGARFTTLYSQAELL 77
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 2-43 2.82e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 40.08  E-value: 2.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 616690648   2 KIAVIGAGVTGlAAAARIASQ-GHEVTIFEKNTNvggRMNQLK 43
Cdd:cd05305  170 KVVILGAGVVG-ENAARVALGlGAEVTVLDINLE---RLRYLD 208
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-501 8.63e-161

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 465.09  E-value: 8.63e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVMMPDVYKDVFTMCGEnyEDYIELR 80
Cdd:COG1233    4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFERPGFRFDVGPSVLTMPGVLERLFRELGL--EDYLELV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  81 QLRYIYDVYFDRDDRITVPTDLAELQHMLESIEPGSTHGFMSFLTDVYKKYEIARRYFLERTYRKPSDFYNMTSLVQGAK 160
Cdd:COG1233   82 PLDPAYRVPFPDGRALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLYRPLLSLRDLLRPLALARLLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 161 LKTLNhADQLIEHYIDNEKIQKLLAFQTLYIGIDPKRGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQLNKDLGVNIE 240
Cdd:COG1233  162 LLLRS-LRDLLRRYFKDPRLRALLAGQALYLGLSPDRTPALYALIAYLEYAGGVWYPKGGMGALADALARLAEELGGEIR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 241 LNAEIEQIIIDPKfkRADAIKV-NGDIRKFDKILCTADFPSVAESLMPDFAPIKKYPpHKIADLDYSCSAFLMYIGIDID 319
Cdd:COG1233  241 TGAEVERILVEGG--RATGVRLaDGEEIRADAVVSNADPAHTYLRLLGEEALPARYR-RRLERFRYSPSAFKLYLGLDGP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 320 VtDQVRLHNVIFSDDFRGNIEEIFEGRLSYDPSIYVYVPAVADKSLAPEGKTGIYVLMPTPelkTGSGIDWsdEALTQQI 399
Cdd:COG1233  318 L-PGLAHHTIHLSEDYEAAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVPVP---YGLEDAW--DELKEEY 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 400 KEIIYRKLAtiEVFEDIKSHIVSETIFTPNDFEQTYHAKFGSAFGLMPTLAQSNYYRPQNVSRDYKDLYFAGASTHPGAG 479
Cdd:COG1233  392 AERILARLE--RYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRPSNYRTPIPGLYLVGASTHPGGG 469

                        490       500
                 ....*....|....*....|..
gi 616690648 480 VPIVLTSAKITVDEMIKDIEQG 501
Cdd:COG1233  470 VPGVLISGRLAARRILKDLKRA 491
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 5-497 8.18e-134

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 396.65  E-value: 8.18e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648    5 VIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVMMPDVYKDVFTMCGENYEDYIELRQLRY 84
Cdd:TIGR02734   3 VIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDDGFRFDTGPTVITMPEALEELFALAGRDLADYVELVPLDP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   85 IYDVYFDRDDRITVPTDLAELQHMLESIEPGSTHGFMSFLTDVYKKYEIARRYFLERTYRKPSDFYNmTSLVQGAKLKTL 164
Cdd:TIGR02734  83 FYRLCWEDGSQLDVDNDQEELEAQIARFNPGDVAGYRRFLDYAERVYREGYRKLGYVPFLSPRDLLR-ADAPQLLALLAW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  165 NHADQLIEHYIDNEKIQKLLAFQTLYIGIDPKRGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQLNKDLGVNIELNAE 244
Cdd:TIGR02734 162 RSLYSKVARFFSDERLRQAFSFHALFLGGNPFRTPSIYALISALEREWGVWFPRGGTGALVAAMAKLAEDLGGELRLNAE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  245 IEQiiIDPKFKRADAIkVNGDIRKF--DKILCTADFPSVAESLMPDfAPIKKYPPHKIADLDYSCSAFLMYIGIDID--V 320
Cdd:TIGR02734 242 VIR--IETEGGRATAV-HLADGERLdaDAVVSNADLHHTYRRLLPN-HPRRRYPAARLSRKRPSPSLFVLYFGLLGVdgH 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  321 TDQVRLHNVIFSDDFRGNIEEIFE-GRLSYDPSIYVYVPAVADKSLAPEGKTGIYVLMPTPELKTGsGIDWSDEAltQQI 399
Cdd:TIGR02734 318 WPQLAHHTLCFGPRYKELFDEIFRkGRLAEDPSLYLHRPTVTDPSLAPPGCESLYVLAPVPHLGTA-DVDWSVEG--PRY 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  400 KEIIYRKLATIEVfEDIKSHIVSETIFTPNDFEQTYHAKFGSAFGLMPTLAQSNYYRPQNVSRDYKDLYFAGASTHPGAG 479
Cdd:TIGR02734 395 RDRILAYLEERAI-PGLRDRIVVERTFTPADFRDRYNAWLGSAFSLEHTLTQSAWFRPHNRDRKIDNLYLVGAGTHPGAG 473

                         490
                  ....*....|....*...
gi 616690648  480 VPIVLTSAKITVDEMIKD 497
Cdd:TIGR02734 474 VPGVLGSAKATAKLMLGD 491
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 10-495 2.58e-26

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 111.04  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   10 VTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVmmPDVYKDVFTMCGE-NYEDYIELRQLRYIYDV 88
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF--HGAQPPLLALLKElGLEDRLVLPDPAPFYTV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   89 YFDRDDRitVPTDLAELQHMLEsiepgsthGFMSFLTDVYKKyEIARRYFLERTYRKPSDFYNMTSLVQGAKLKTLNH-- 166
Cdd:pfam01593  79 LFAGGRR--YPGDFRRVPAGWE--------GLLEFGRLLSIP-EKLRLGLAALASDALDEFDLDDFSLAESLLFLGRRgp 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  167 -ADQLIEHYIDNEKIQKLLAFQTLYIGIDPK--RGPSLYSIIPMIEMMFGVHFIKGGMYGMAQGLAQlnKDLGVNIELNA 243
Cdd:pfam01593 148 gDVEVWDRLIDPELFAALPFASGAFAGDPSElsAGLALPLLWALLGEGGSLLLPRGGLGALPDALAA--QLLGGDVRLNT 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  244 EIEQIIidpkfKRADAIKV---NGDIRKFDKILCTADfPSVAESLMPDfAPIKKYPPHKIADLDY--SCSAFLMYigidi 318
Cdd:pfam01593 226 RVRSID-----REGDGVTVtltDGEVIEADAVIVTVP-LGVLKRILFT-PPLPPEKARAIRNLGYgpVNKVHLEF----- 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  319 dvtDQVRLHNvifsDDFRGNIEEIFEGRlsydPSIYVYVPavaDKSLAPEGKTGIYVLMptpelkTGSGiDW-------S 391
Cdd:pfam01593 294 ---DRKFWPD----LGLLGLLSELLTGL----GTAFSWLT---FPNRAPPGKGLLLLVY------VGPG-DRareleglS 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  392 DEALTQQIKEIIyRKLATIEVFEDIKSHIVSetiFTPNDFeqtyhakFGSAFGLMPTLAQSNYYRPQNVSRDyKDLYFAG 471
Cdd:pfam01593 353 DEELLQAVLRDL-RKLFGEEAPEPLRVLVSD---WHTDPW-------PRGSYSLPQYGPGHDDYRPLARTPD-PGLFFAG 420

                         490       500
                  ....*....|....*....|....*.
gi 616690648  472 ASTHPG--AGVPIVLTSAKITVDEMI 495
Cdd:pfam01593 421 EHTSTGypGTVEGAIESGRRAARAVL 446
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-421 1.81e-18

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: 87.58  E-value: 1.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVMMPDvyKDVFTMCGE-NYEDYIEL 79
Cdd:COG1232    2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD--PEVLELLRElGLGDELVW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  80 RQ--LRYIYdvyfdRDDRitvptdlaeLQHMLESIEPGSTHGFMSFLTdvykKYEIARRYFLERTYRKPSDfyNMTSLVQ 157
Cdd:COG1232   80 PNtrKSYIY-----YGGK---------LHPLPQGPLALLRSPLLSLAG----KLRALLELLAPRRPPGEDE--SLAEFVR 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 158 ---GAKLktlnhADQLIE------HYIDNEKIQKLLAFQTLYiGIDPKRGpSLysIIPMIEMMFG------VHFIKGGMY 222
Cdd:COG1232  140 rrfGREV-----YERLVEpllegvYAGDPDELSADWAFPRLK-RLELEHG-SL--IKGALALRKGakagevFGYLRGGLG 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 223 GMAQGLAQlnkDLG-VNIELNAEIEQIIIDPKFKRADAikVNGDIRKFDKILCTADFPsVAESLMPDFAPikkYPPHKIA 301
Cdd:COG1232  211 TLVEALAE---ALEaGEIRLGTRVTAIEREGGGWRVTT--SDGETIEADAVVSATPAP-ALARLLAPLPP---EVAAALA 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 302 DLDYSCSAfLMYIGIDIDVTDQVRLHNVIFSDDfrgniEEIFEGRLSYdPSiyVYVPAvadksLAPEGKTGIYVLMP--- 378
Cdd:COG1232  282 GIPYASVA-VVALGFDRPDLPPPDGFGWLVPRD-----EGVPILAVTF-SS--NKWPH-----RAPDGKVLLRLEVGgag 347

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 616690648 379 TPELktgsgIDWSDEALTQQ-IKEIiyRKLATIEVfEDIKSHIV 421
Cdd:COG1232  348 DPEL-----WQLSDEELVALaLADL--RKLLGIDA-EPVDTRVV 383
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-52 9.69e-15

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 75.30  E-value: 9.69e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMG 52
Cdd:COG3380    4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRLDGGRFDHG 55
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
5-71 8.43e-14

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 66.02  E-value: 8.43e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690648    5 VIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIvMMPDVYKDVFTMCGE 71
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPGYVFDYGAHI-FHGSDEPNVRDLLDE 66
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
2-291 9.15e-12

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 66.87  E-value: 9.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRM--NQLKKDGFTFDMGPTivMMPDVYKDVFTMCGE---NYEDY 76
Cdd:COG1231    9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVwtLRFGDDGLYAELGAM--RIPPSHTNLLALARElglPLEPF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648  77 IELRQLRYIY--DVYFDRDDRITVPTDLAEL-----QHMLESIEPGSThgfmsfLTDVYKKYEIARryFLERtyrkpsdf 149
Cdd:COG1231   87 PNENGNALLYlgGKRVRAGEIAADLRGVAELlakllRALAAALDPWAH------PAAELDRESLAE--WLRR-------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648 150 ynmtslvQGAklktLNHADQLIEHYIdnekiqkllafqTLYIGIDPKRgpslYSIIPMIEMMFGVHF------IKGGMYG 223
Cdd:COG1231  151 -------NGA----SPSARRLLGLLG------------AGEYGADPDE----LSLLDLLRYAASAGGgaqqfrIVGGMDQ 203

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690648 224 MAQGLAqlnKDLGVNIELNAEIEQIIidpkfKRADAIKV---NGDIRKFDKILCTADfPSVAESLmpDFAP 291
Cdd:COG1231  204 LPRALA---AELGDRIRLGAPVTRIR-----QDGDGVTVttdDGGTVRADAVIVTVP-PSVLRRI--EFDP 263
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 1-53 4.17e-11

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 64.87  E-value: 4.17e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQG--HEVTIFEKNTNVGGRMNQLKKDGFTFDMGP 53
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKDGFPIELGP 55
PRK07233 PRK07233
hypothetical protein; Provisional
 2-37 2.96e-10

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 62.21  E-value: 2.96e-10
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
2-68 4.20e-10

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 62.18  E-value: 4.20e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIV--MMPDVYKD----VFTM 68
Cdd:COG1148  142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPGLDCPQCILepLIAEVEANpnitVYTG 214
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 1-37 1.66e-09

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 59.81  E-value: 1.66e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 2-37 2.04e-09

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 59.38  E-value: 2.04e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:COG0493  123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 2-49 3.68e-09

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 59.02  E-value: 3.68e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG------------------RMNQLKKDGFTF 49
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGllrygipdfklekevidrRIELMEAEGIEF 210
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 2-105 6.92e-09

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 57.92  E-value: 6.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648    2 KIAVIGAGVTGLAAAARIASQ----GHEVTIFEKNTNVGGRMNQLKKDGFTFDMGPTIVM-----MPDVYKDVftmcgeN 72
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLEKEipelPVELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLerkksAPDLVKDL------G 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 616690648   73 YEDYIELRQLRYIYdVYFDRDDRITVPTDLAEL 105
Cdd:TIGR00562  78 LEHVLVSDATGQRY-VLVNRGKLMPVPTKIAPF 109
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
1-37 7.08e-09

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 57.82  E-value: 7.08e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQgHEVTIFEKNTNVGG 37
Cdd:COG2907    4 MRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 1-38 1.79e-08

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 56.79  E-value: 1.79e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGR 38
Cdd:COG3349    4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGR 41
PRK06753 PRK06753
hypothetical protein; Provisional
 1-35 4.72e-08

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 55.08  E-value: 4.72e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNV 35
Cdd:PRK06753   1 MKIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
PLN02487 PLN02487
zeta-carotene desaturase
 1-52 1.10e-07

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 54.42  E-value: 1.10e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLK-KDGFTFDMG 52
Cdd:PLN02487  76 LKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFVdKNGNHIEMG 128
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 2-39 1.80e-07

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 53.73  E-value: 1.80e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRM 39
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMM 176
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 2-127 4.17e-07

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 52.42  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQ------LKKDGFTFDMGPTIVMMPDVykdVF-TMCGENye 74
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYgiprfrLPESVIDADIAPLRAMGAEF---RFnTVFGRD-- 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 616690648  75 dyIELRQLRYIYDVYFdrddrITVPTDLAELQHMLESIEPGSTHGfMSFLTDV 127
Cdd:PRK12814 270 --ITLEELQKEFDAVL-----LAVGAQKASKMGIPGEELPGVISG-IDFLRNV 314
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-33 4.55e-07

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 51.83  E-value: 4.55e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNT 33
Cdd:COG0665    3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGR 35
PLN02576 PLN02576
protoporphyrinogen oxidase
 4-53 7.30e-07

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 51.55  E-value: 7.30e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 616690648   4 AVIGAGVTGLAAAARIASQ-GHEVTIFEKNTNVGGRMNQLKKDGFTFDMGP 53
Cdd:PLN02576  16 AVVGAGVSGLAAAYALASKhGVNVLVTEARDRVGGNITSVSEDGFIWEEGP 66
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 3-37 8.28e-07

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: 51.40  E-value: 8.28e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 616690648   3 IAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:COG2072    9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 2-37 1.22e-06

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: 50.47  E-value: 1.22e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 616690648    2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-52 1.39e-06

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: 50.24  E-value: 1.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKntnvGGRMNQLKKDGFTFDMG 52
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTLVAR----GAHAEALRENGLRLESP 48
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-33 1.41e-06

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 50.32  E-value: 1.41e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNT 33
Cdd:COG0654    4 TDVLIVGGGPAGLALALALARAGIRVTVVERAP 36
PRK07208 PRK07208
hypothetical protein; Provisional
 2-52 1.55e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 50.66  E-value: 1.55e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMG 52
Cdd:PRK07208   6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKGNRFDIG 56
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 2-39 6.95e-06

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 48.06  E-value: 6.95e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRM 39
Cdd:PRK12770  20 KVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLM 57
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 1-53 7.43e-06

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 48.15  E-value: 7.43e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMGP 53
Cdd:COG0771    5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELAAAELEAPGVEVVLGE 57
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-59 8.86e-06

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 47.54  E-value: 8.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFeknTNVGGRMNQLKKDGFTFDMGPTIVMMP 59
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLV---ARRGAHLDALNENGLRLEDGEITVPVL 56
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-44 9.86e-06

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 47.99  E-value: 9.86e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 616690648    1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNtnvGGRMNQLKK 44
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDID---QEKVDKLNK 41
PRK13984 PRK13984
putative oxidoreductase; Provisional
 2-90 1.07e-05

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 48.22  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMN-----------QLKKD-GFTFDMGPTIVMMPDVYKDvftmc 69
Cdd:PRK13984 285 KVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRygipsyrlpdeALDKDiAFIEALGVKIHLNTRVGKD----- 359

                         90       100
                 ....*....|....*....|.
gi 616690648  70 genyedyIELRQLRYIYDVYF 90
Cdd:PRK13984 360 -------IPLEELREKHDAVF 373
HI0933_like pfam03486
HI0933-like protein;
2-40 1.71e-05

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 47.19  E-value: 1.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 616690648    2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVG--------GRMN 40
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGrkilisggGRCN 48
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 1-37 1.81e-05

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 47.43  E-value: 1.81e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:PRK12778 432 KKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
PRK12831 PRK12831
putative oxidoreductase; Provisional
 1-30 2.04e-05

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 46.93  E-value: 2.04e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFE 30
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFE 170
PLN02568 PLN02568
polyamine oxidase
 2-54 6.65e-05

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 45.59  E-value: 6.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGH-----EVTIFEKNTNVGGRMNQLKKDGFTFDMGPT 54
Cdd:PLN02568   7 RIVIIGAGMAGLTAANKLYTSSAandmfELTVVEGGDRIGGRINTSEFGGERIEMGAT 64
PLN02268 PLN02268
probable polyamine oxidase
 5-52 7.41e-05

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 45.06  E-value: 7.41e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 616690648   5 VIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQLKKDGFTFDMG 52
Cdd:PLN02268   5 VIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSFGFPVDMG 52
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 2-32 1.23e-04

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 44.24  E-value: 1.23e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKN 32
Cdd:PRK12409   3 HIAVIGAGITGVTTAYALAQRGYQVTVFDRH 33
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
1-36 1.23e-04

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 44.56  E-value: 1.23e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGH---EVTIFEKNTNVG 36
Cdd:COG4529    6 KRIAIIGGGASGTALAIHLLRRAPeplRITLFEPRPELG 44
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-49 1.48e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 42.11  E-value: 1.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 616690648     2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNV--------GGRMNQLKKDGFTF 49
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARlrqlesllGARFTTLYSQAELL 77
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
 2-76 1.82e-04

Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.


Pssm-ID: 395602 [Multi-domain]  Cd Length: 531  Bit Score: 44.00  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648    2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG--RMNQLKKDGftfdmgptivmMPDVYKDVFT------MCGENY 73
Cdd:pfam00743   3 KVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGlwRFTENVEEG-----------RASIYKSVITntskemSCFSDF 71


                  ....*.
gi 616690648   74 ---EDY 76
Cdd:pfam00743  72 pfpEDY 77
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-39 2.18e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 43.08  E-value: 2.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 616690648    1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTN-VGGRM 39
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcPYGGC 40
PRK00711 PRK00711
D-amino acid dehydrogenase;
1-30 2.23e-04

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 43.63  E-value: 2.23e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFE 30
Cdd:PRK00711   1 MRVVVLGSGVIGVTSAWYLAQAGHEVTVID 30
PLN02976 PLN02976
amine oxidase
 2-38 2.42e-04

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 44.09  E-value: 2.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 616690648    2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGR 38
Cdd:PLN02976  695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGR 731
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 3-37 3.32e-04

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: 43.05  E-value: 3.32e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 616690648    3 IAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-56 3.91e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 42.31  E-value: 3.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690648    2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQ---------LKKDGFTFDMGPTIV 56
Cdd:pfam07992 154 RVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEeisaalekaLEKNGVEVRLGTSVK 217
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 3-37 5.77e-04

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 42.16  E-value: 5.77e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 616690648   3 IAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:PLN02172  13 VAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
1-41 6.05e-04

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 42.32  E-value: 6.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGGRMNQ 41
Cdd:COG1004    1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNA 41
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-48 6.18e-04

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 40.53  E-value: 6.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 616690648    2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTnvgGRMNQLKKDGFT 48
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTP---EKVEELVAAGAI 44
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-29 6.75e-04

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 41.64  E-value: 6.75e-04
                         10        20
                 ....*....|....*....|....*....
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIF 29
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVW 30
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
3-36 7.41e-04

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 42.06  E-value: 7.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 616690648   3 IAVIGAGVTGLAAAARIA-SQGHEVTIFEKNTNVG 36
Cdd:COG0579    7 VVIIGAGIVGLALARELSrYEDLKVLVLEKEDDVA 41
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 1-27 8.43e-04

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 40.31  E-value: 8.43e-04
                          10        20
                  ....*....|....*....|....*..
gi 616690648    1 MKIAVIGAGVTGLAAAARIASQGHEVT 27
Cdd:pfam03721   1 MKISVIGLGYVGLPTAACLAEIGHDVI 27
PRK07236 PRK07236
hypothetical protein; Provisional
 1-123 9.87e-04

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 41.45  E-value: 9.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTnvggrmNQLkkDGFtfdmGPTIVMMPDVYkDVFTMCGENYEDYIELR 80
Cdd:PRK07236   7 PRAVVIGGSLGGLFAALLLRRAGWDVDVFERSP------TEL--DGR----GAGIVLQPELL-RALAEAGVALPADIGVP 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690648  81 QLRYIydvYFDRDDRI----------------------TVPTDLAELQHMLESIEPGSTHGFMSF 123
Cdd:PRK07236  74 SRERI---YLDRDGRVvqrrpmpqtqtswnvlyralraAFPAERYHLGETLVGFEQDGDRVTARF 135
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 2-31 9.97e-04

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: 41.76  E-value: 9.97e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEK 31
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEA 291
PRK07538 PRK07538
hypothetical protein; Provisional
 1-30 1.00e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 41.42  E-value: 1.00e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFE 30
Cdd:PRK07538   1 MKVLIAGGGIGGLTLALTLHQRGIEVVVFE 30
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
 2-52 1.86e-03

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 40.72  E-value: 1.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNT--NVGGRMNQLKKDGFTFDMG 52
Cdd:PRK14106   7 KVLVVGAGVSGLALAKFLKKLGAKVILTDEKEedQLKEALEELGELGIELVLG 59
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 2-35 1.89e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 39.79  E-value: 1.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 616690648    2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNV 35
Cdd:pfam01262  30 KVLVIGGGVAGLNAAATAKGLGAIVTILDVRPAR 63
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 1-32 1.96e-03

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: 40.09  E-value: 1.96e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKN 32
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDIS 34
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-49 2.45e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 40.05  E-value: 2.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNvggRMNQLKKDGFTF 49
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPE---RVERLAEEDVLV 141
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 3-37 2.79e-03

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 40.59  E-value: 2.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 616690648   3 IAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGG 343
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 2-43 2.82e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 40.08  E-value: 2.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 616690648   2 KIAVIGAGVTGlAAAARIASQ-GHEVTIFEKNTNvggRMNQLK 43
Cdd:cd05305  170 KVVILGAGVVG-ENAARVALGlGAEVTVLDINLE---RLRYLD 208
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 5-37 3.34e-03

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: 39.82  E-value: 3.34e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 616690648   5 VIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:COG1053    8 VVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
8-38 4.22e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.18  E-value: 4.22e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 616690648   8 AGVTGLAAAARIASQGHEVTIFEKNTNVGGR 38
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDK 31
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-41 5.10e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 38.90  E-value: 5.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 616690648   1 MKIAVIGAGV--TGLAAAAriASQGHEVTIFEKNTNVGGRMNQ 41
Cdd:PRK00094   2 MKIAVLGAGSwgTALAIVL--ARNGHDVTLWARDPEQAAEINA 42
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
2-50 5.16e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 39.25  E-value: 5.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 616690648   2 KIAVIGAGVTGLAAAARIASQGHEVTIFEKNTNVG--GRMNQLKKDGF-TFD 50
Cdd:PRK08163   6 PVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGeiGAGIQLGPNAFsALD 57
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
3-27 6.62e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 38.73  E-value: 6.62e-03
                         10        20
                 ....*....|....*....|....*
gi 616690648   3 IAVIGAGVTGLAAAARIASQGHEVT 27
Cdd:PRK07494  10 IAVIGGGPAGLAAAIALARAGASVA 34
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 3-37 6.63e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 38.91  E-value: 6.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 616690648   3 IAVIGAGVTGLAAAARIASQGHEVTIFEKNTnVGG 37
Cdd:COG1249    6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGG 39
PRK07588 PRK07588
FAD-binding domain;
1-31 6.74e-03

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 38.95  E-value: 6.74e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 616690648   1 MKIAVIGAGVTGLAAAARIASQGHEVTIFEK 31
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIER 31
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
 5-37 7.55e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 38.93  E-value: 7.55e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 616690648   5 VIGAGVTGLAAAARIASQGHEVTIFEKNTNVGG 37
Cdd:PRK06134  17 VIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
NAD_binding_9 pfam13454
FAD-NAD(P)-binding;
4-38 9.13e-03

FAD-NAD(P)-binding;


Pssm-ID: 433222 [Multi-domain]  Cd Length: 155  Bit Score: 36.87  E-value: 9.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 616690648    4 AVIGAGVTGLAAAARIASQ----GHEVTIFEKNTNVGGR 38
Cdd:pfam13454   1 AIVGGGPSGLALLERLLARapkrPLEITLFDPSPPGAGG 39
 
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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