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Conserved domains on  [gi|446380986|ref|WP_000458841|]
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hydroxylamine reductase [Escherichia coli]

Protein Classification

hydroxylamine reductase( domain architecture ID 10012303)

hydroxylamine reductase contains a hybrid [Fe4-S2-O2] cluster; it catalyzes the reduction of hydroxylamine to form ammonia and water

EC:  1.7.99.1
Gene Symbol:  hcp
Gene Ontology:  GO:0050418|GO:0046872|GO:0051537
PubMed:  9667933|10651802
SCOP:  4002941

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK05290 PRK05290
hybrid cluster protein; Provisional
1-550 0e+00

hybrid cluster protein; Provisional


:

Pssm-ID: 235391  Cd Length: 546  Bit Score: 1010.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTIRtpaGNGCsYAQGMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINHDVDSFAPRAFFSTLTNVNFD 80
Cdd:PRK05290   1 MFCYQCEQTAR---GNGC-TAQGVCGKTAETADLQDLLIYALKGLSAYALKARELGIIDHEVDRFVPEALFTTLTNVNFD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  81 SPRIIGYAREAIALREALKAQCLAvDANARVDNPMADLQLVSDDLGELQRQAAEFTPNKDkAAIGENILGLRLLCLYGLK 160
Cdd:PRK05290  77 DERIVGYIKEAIALREALKAKLAA-DGNAPEDLPDAALWLPADDLEELLAQAAEVGVLAD-ATENEDIRSLRELLLYGLK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 161 GAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:PRK05290 155 GMAAYAEHARVLGQTDEEIYAFYHKALAALGDDPLDVDELLALVLECGKMNVKVMALLDKANTETYGHPEPTKVNIGVRK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:PRK05290 235 GPGILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLVGNYGSAWQNQQKEFASFPGPILMTTNCIIP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 321 PTvGAYDDRIWTRSIVGWPGVRHLDGE---DFSAVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLR 397
Cdd:PRK05290 315 PK-GSYKDRIFTTGIVGWPGVKHIEGDgkkDFSPVIEKALELPGFPPDEIEHEITVGFAHNAVLAVADKVIDAVKSGAIR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 398 HIFLLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGC 477
Cdd:PRK05290 394 HFFLMGGCDGAKPGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGIPRLLDAGQCNDAYSAIVIALALAEAFGC 473
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446380986 478 GVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLLSA 550
Cdd:PRK05290 474 DVNDLPLSLVLSWYEQKAVAVLLTLLSLGVKNIRLGPTLPAFLSPNVLKVLVEKFGIRPITTVEEDLKAILGA 546
 
Name Accession Description Interval E-value
PRK05290 PRK05290
hybrid cluster protein; Provisional
1-550 0e+00

hybrid cluster protein; Provisional


Pssm-ID: 235391  Cd Length: 546  Bit Score: 1010.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTIRtpaGNGCsYAQGMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINHDVDSFAPRAFFSTLTNVNFD 80
Cdd:PRK05290   1 MFCYQCEQTAR---GNGC-TAQGVCGKTAETADLQDLLIYALKGLSAYALKARELGIIDHEVDRFVPEALFTTLTNVNFD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  81 SPRIIGYAREAIALREALKAQCLAvDANARVDNPMADLQLVSDDLGELQRQAAEFTPNKDkAAIGENILGLRLLCLYGLK 160
Cdd:PRK05290  77 DERIVGYIKEAIALREALKAKLAA-DGNAPEDLPDAALWLPADDLEELLAQAAEVGVLAD-ATENEDIRSLRELLLYGLK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 161 GAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:PRK05290 155 GMAAYAEHARVLGQTDEEIYAFYHKALAALGDDPLDVDELLALVLECGKMNVKVMALLDKANTETYGHPEPTKVNIGVRK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:PRK05290 235 GPGILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLVGNYGSAWQNQQKEFASFPGPILMTTNCIIP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 321 PTvGAYDDRIWTRSIVGWPGVRHLDGE---DFSAVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLR 397
Cdd:PRK05290 315 PK-GSYKDRIFTTGIVGWPGVKHIEGDgkkDFSPVIEKALELPGFPPDEIEHEITVGFAHNAVLAVADKVIDAVKSGAIR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 398 HIFLLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGC 477
Cdd:PRK05290 394 HFFLMGGCDGAKPGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGIPRLLDAGQCNDAYSAIVIALALAEAFGC 473
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446380986 478 GVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLLSA 550
Cdd:PRK05290 474 DVNDLPLSLVLSWYEQKAVAVLLTLLSLGVKNIRLGPTLPAFLSPNVLKVLVEKFGIRPITTVEEDLKAILGA 546
hybrid_clust TIGR01703
hydroxylamine reductase; This model represents a family of proteins containing an unusual ...
1-548 0e+00

hydroxylamine reductase; This model represents a family of proteins containing an unusual 4Fe-2S-2O hydrid cluster. Earlier reports had proposed a 6Fe-6S prismane cluster. This subfamily is heterogeneous with respect to the presence or absence of a region of about 100 amino acids not far from the N-terminus of the protein. Members have been described as monomeric. The general function is unknown, although members from E. coli and several other species have hydroxylamine reductase activity. Members are found in various bacteria, in Archaea, and in several parasitic eukaryotes: Giardia intestinalis, Trichomonas vaginalis, and Entamoeba histolytica. [Cellular processes, Detoxification, Energy metabolism, Amino acids and amines]


Pssm-ID: 130764  Cd Length: 522  Bit Score: 787.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986    1 MFCVQCEQTIRtpaGNGCSyAQGMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINhDVDSFAPRAFFSTLTNVNFD 80
Cdd:TIGR01703   1 MFCYQCEQTAR---GTGCT-VRGVCGKDPETANLQDLLVYVLKGISLWALQARKLGIDS-EIDSFIPRALFSTLTNVNFD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   81 SPRIIGYAREAIALREALKAQCLAVDANArvdnpmadlqlvsddlgeLQRQAaeFTPNKDKAAIGENILGLRLLCLYGLK 160
Cdd:TIGR01703  76 EDRIVEYIEDAIKLREKLKKKCRLADSNS------------------LLIQS--FALNGDKSHVNDDVNSLRDLLLYGIK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  161 GAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:TIGR01703 136 GIAAYLYHARELGYDDEEIYAFLEEALASTLTNVFDADELIDLALEVGKMNLEAMKLLDKANTETYGLPEPTEVNIGTTE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:TIGR01703 216 GKAILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLAGNYGGAWQDQQREFAEFPGPILMTSNCIIP 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  321 PTVgAYDDRIWTRSIVGWPGVRHLDGEDFSAVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIF 400
Cdd:TIGR01703 296 PRK-SYKDRIFTTGIVGWPGVKHIENYDFSPVIEKALELPGFPKELEEGTITTGFGHHTILALADKIVELVKEGKIRHFF 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  401 LLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVN 480
Cdd:TIGR01703 375 LVGGCDGPNPERNYYTEFARKLPKDAIILTLACGKYRFNKLDLGDIEGIPRLLDLGQCNDAYSAIEIALKLAEVFGCDVN 454
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446380986  481 DLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLL 548
Cdd:TIGR01703 455 ELPLSIVLSWYEQKAIAILLALLYLGVKNIYIGPTLPGFLTPNVFKILVDNFDLRLIGEPEDDLRAIL 522
HCP cd01914
Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in ...
1-548 0e+00

Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. HCP has three structural domains, an N-terminal alpha-helical domain, and two similar domains comprising a central beta-sheet flanked by alpha-helices. HCP contains two iron-sulfur clusters, one of which is a [Fe4-S4] cubane cluster similar to that of carbon monoxide dehydrogenase (CODH). The second cluster, referred to as the hybrid cluster, is a hybrid [Fe4-S2-O2] center located at the interface of the three domains. Although the hybrid cluster is buried within the protein, it is accessible through a large hydrophobic cavity.


Pssm-ID: 238895  Cd Length: 423  Bit Score: 732.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTIRtpaGNGCSYAqGMCGKTAETSDLQDlliatlqglsawavkareygiinhdvdsfapraffstltnvnfd 80
Cdd:cd01914    1 MFCYQCEQTAK---GTGCTVR-GVCGKDPEVANLQD-------------------------------------------- 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  81 spriigyareaialrealkaqclavdanarvdnpmadlqlvsddlgelqrqaaeftpnkdkaaigenilglrllclYGLK 160
Cdd:cd01914   33 ----------------------------------------------------------------------------YGLK 36
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 161 GAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:cd01914   37 GIAAYAEHARVLGYDDEEIYAFIEKALASLLDNPLDADELLALALETGRMNLKVMELLDKANTETYGHPEPTEVNIGVRA 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:cd01914  117 GKGILVSGHDLKDLEELLEQTEGTGVDVYTHGEMLPAHGYPELKKYPHLVGNYGGAWQNQQKEFARFPGPILMTTNCIIP 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 321 PTvGAYDDRIWTRSIVGWPGVRHLDGEDFSAVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIF 400
Cdd:cd01914  197 PR-ESYKDRIFTTGIVGWPGVKHIEGKDFSEVIEKAKELPGFPEEEESGTITTGFAHNQVLAVADKVVEAVKSGKIRHFF 275
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 401 LLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVN 480
Cdd:cd01914  276 VVGGCDGRHKGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGIPRLLDAGQCNDSYSAIVIALALAEAFGCDVN 355
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446380986 481 DLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLL 548
Cdd:cd01914  356 DLPLSLVLSWYEQKAVAVLLALLALGVKNIRLGPTLPAFLTPNVLKVLVENFGLKPIGTVEEDLKAIL 423
Prismane pfam03063
Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the ...
1-545 0e+00

Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the beta chain of carbon monoxide dehydrogenase. The hybrid-cluster proteins contain two Fe/S centres - a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster. The physiological role of this protein is as yet unknown, although a role in nitrate/nitrite respiration has been suggested. The prismane protein from Escherichia coli was shown to contain hydroxylamine reductase activity (NH2OH + 2e + 2 H+ -> NH3 + H2O). This activity is rather low. Hydroxylamine reductase activity was also found in CO-dehydrogenase in which the active site Ni was replaced by Fe. The CO dehydrogenase contains a Ni-3Fe-2S-3O centre.


Pssm-ID: 460790 [Multi-domain]  Cd Length: 539  Bit Score: 577.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986    1 MFCVQCEqtirtpaGNGCSYAQ---GMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINHDvdsfaprAFFSTLTNV 77
Cdd:pfam03063   1 MFCRQCE-------MGPCRITPkprGVCGKTADTIVARNLLRYVAAGAAAHSDHARELGLTLKE-------ALFGTLTNY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   78 NFDSPRIIGYAREAIALREALKaqclavdanarvdnpmadlqlvsdDLGELQRQAAEFTPNkDKAAIGENILGLRLLCLY 157
Cdd:pfam03063  67 NIDDERKLKRIAEALGIRTELK------------------------DIEELAAEVADVGLE-DFYGKNEDIRSLRELAPY 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  158 GLKGAAAymEHAHVLGQYDNDIYAQYHKIMAWLGTWPADmnaLLECSMEIGQMNFKVMSILDAGETGKYGHPTP--TQVN 235
Cdd:pfam03063 122 GRKGLWA--EHAIVPGGIDREVFEFMHRTLTGLDSDPLD---LLLLALRCGLADLGGMELLDEANDILFGTPEPvlTEVN 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  236 --VKATAGKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELR-KFKHLVGNYGSGWQNQQVEFARFPGPIV 312
Cdd:pfam03063 197 lgVLDKDYVNILVSGHDPKDLEMLLEQTEGTGINVYAHGEMLPGHCCPGLKlKYRHGVGNYGNAWQQELAEFTGFPDAIV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  313 MTSNCIIDP---TVGAYDDRIWTRSIVGW-PGVRHLD------GEDFSAVIAQAQQMAGFP---YSEIPHLITVGFG--- 376
Cdd:pfam03063 277 VDTNCIMPPlasVASCYHTRLITTSPVGKiPGATHIEfdeekaDKDASEIIEKAIEAFKFReieKVEIPGEKVGGVAgfs 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  377 ----RQTLLGAADTLIDLVSREKLRHIFLLGGCDGARGERHYFTDFATSV-PDDCLILTLACGKYRFNKLEFGDIE---- 447
Cdd:pfam03063 357 teaiHEAVLGSADPLIDAIKSGAIRGFVLVVGCDNAKPGRDYYTELAKELiPKDILVLTTGCAKYRFNKLGLGDIEaael 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  448 ---GLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPL-SLVLSWFEQKAIVILLTLLSLGVkNIVTGPTAPGFLTPD 523
Cdd:pfam03063 437 agdGLPPVLDMGQCNDNYRAIVIALALAEALGVDINDLPLaSSAPEWYEQKAVAIGLTLLALGI-NIHLGPTPPAFGSPN 515
                         570       580
                  ....*....|....*....|....
gi 446380986  524 LLAVLNEKF--GLRSITTVEEDMK 545
Cdd:pfam03063 516 VLKVLTENFedLIGGIFTVEEDPK 539
Hcp COG1151
Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion];
1-548 1.98e-173

Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion];


Pssm-ID: 440765  Cd Length: 613  Bit Score: 503.58  E-value: 1.98e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTirtpagnGCSY----AQGMCGKTAETSDLQDLLIATLQGLSAWAVKARE-------------YGIINHDVD 63
Cdd:COG1151   38 MCCRQCEQG-------PCRItpktPRGVCGKTADTIVARNLLRYVAKGAAAHADHAREvaltlkaaaegadYEIKDEEKL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  64 SFAPRAFFSTltnvnfdsPRIIGYAREAIALREALKAQClavdanARVDNPMADLqlvsddlgeLQRQAAEftpnkdkaa 143
Cdd:COG1151  111 RFVAEALGIT--------TEGKDLIEIALELADALLEDF------GKAGGEPATW---------LEAKAPE--------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 144 igENILGLRLLclyglkgaaaymehahvlGQYDNDIYAQYHKIMAWLGT-WPADMNALLECSMEIGQMNFKVMSILDAGE 222
Cdd:COG1151  159 --ERIESWREL------------------GIEPRGIDREIVEALARTHTgVDLDPVNLLLLALRTGLADWGGMALLDEAN 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 223 TGKYGHPTPTQVN----VKATAGKCILISGHDLK----------DLYNLLEQTEGTGVNVY----THGEMLPAHGYPElR 284
Cdd:COG1151  219 DILFGTPEPTEVEvnlgVLKEDGVNILVHGHDPKlseaiveaarDLEELAKQTGAKGINVYgiccTGGEMLPRHGYPE-K 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 285 KFKHLVGNYGSGwqnqqvEFARFPGPI---VMTSNCIIDP----TVGAYDDRIWTRSIVGWPGVRHLDG------EDFSA 351
Cdd:COG1151  298 KYVHLAGNYGSA------EFAIFTGAIdamVVDTNCIMPPlasvAECYYTDRITTTGVVGIPGAEHIEFdeegalEDASE 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 352 VIAQAQQMAGFPYSEIPHL------ITVGFGRQTLLGA---ADTLIDLVSREKLRHIFLLGGCDGARGER--HYFTDFAT 420
Cdd:COG1151  372 IIEKAIENFKPREDEKVYIpqekgeIVVGFSHEAVLAAlgsADPLIDAIKSGKIRGFVLVVGCDGRKPGRdyNYYTLFKE 451
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 421 SVPDDCLILTLACGKYRFNKLEFGDIE----------------GLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPL 484
Cdd:COG1151  452 LIPNDVLVLTTGCAKYRLNKLGLGDIEaaelageglkevcealGIPPVLDMGQCNDNYRALVLALALAEALGVDINDLPL 531
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446380986 485 SLVL-SWFEQKAIVILLTLLSLGVKnIVTGPTAPGFLTPDLLAVLNEKF-GLRSIT-TVEEDMKQLL 548
Cdd:COG1151  532 AGSApEWYEQKAVAIGLYLLALGVK-IHLGPTPPAFGSPNVLKVLTEDFeDITGGTfTVEEDPKKAA 597
 
Name Accession Description Interval E-value
PRK05290 PRK05290
hybrid cluster protein; Provisional
1-550 0e+00

hybrid cluster protein; Provisional


Pssm-ID: 235391  Cd Length: 546  Bit Score: 1010.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTIRtpaGNGCsYAQGMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINHDVDSFAPRAFFSTLTNVNFD 80
Cdd:PRK05290   1 MFCYQCEQTAR---GNGC-TAQGVCGKTAETADLQDLLIYALKGLSAYALKARELGIIDHEVDRFVPEALFTTLTNVNFD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  81 SPRIIGYAREAIALREALKAQCLAvDANARVDNPMADLQLVSDDLGELQRQAAEFTPNKDkAAIGENILGLRLLCLYGLK 160
Cdd:PRK05290  77 DERIVGYIKEAIALREALKAKLAA-DGNAPEDLPDAALWLPADDLEELLAQAAEVGVLAD-ATENEDIRSLRELLLYGLK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 161 GAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:PRK05290 155 GMAAYAEHARVLGQTDEEIYAFYHKALAALGDDPLDVDELLALVLECGKMNVKVMALLDKANTETYGHPEPTKVNIGVRK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:PRK05290 235 GPGILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLVGNYGSAWQNQQKEFASFPGPILMTTNCIIP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 321 PTvGAYDDRIWTRSIVGWPGVRHLDGE---DFSAVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLR 397
Cdd:PRK05290 315 PK-GSYKDRIFTTGIVGWPGVKHIEGDgkkDFSPVIEKALELPGFPPDEIEHEITVGFAHNAVLAVADKVIDAVKSGAIR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 398 HIFLLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGC 477
Cdd:PRK05290 394 HFFLMGGCDGAKPGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGIPRLLDAGQCNDAYSAIVIALALAEAFGC 473
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446380986 478 GVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLLSA 550
Cdd:PRK05290 474 DVNDLPLSLVLSWYEQKAVAVLLTLLSLGVKNIRLGPTLPAFLSPNVLKVLVEKFGIRPITTVEEDLKAILGA 546
hybrid_clust TIGR01703
hydroxylamine reductase; This model represents a family of proteins containing an unusual ...
1-548 0e+00

hydroxylamine reductase; This model represents a family of proteins containing an unusual 4Fe-2S-2O hydrid cluster. Earlier reports had proposed a 6Fe-6S prismane cluster. This subfamily is heterogeneous with respect to the presence or absence of a region of about 100 amino acids not far from the N-terminus of the protein. Members have been described as monomeric. The general function is unknown, although members from E. coli and several other species have hydroxylamine reductase activity. Members are found in various bacteria, in Archaea, and in several parasitic eukaryotes: Giardia intestinalis, Trichomonas vaginalis, and Entamoeba histolytica. [Cellular processes, Detoxification, Energy metabolism, Amino acids and amines]


Pssm-ID: 130764  Cd Length: 522  Bit Score: 787.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986    1 MFCVQCEQTIRtpaGNGCSyAQGMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINhDVDSFAPRAFFSTLTNVNFD 80
Cdd:TIGR01703   1 MFCYQCEQTAR---GTGCT-VRGVCGKDPETANLQDLLVYVLKGISLWALQARKLGIDS-EIDSFIPRALFSTLTNVNFD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   81 SPRIIGYAREAIALREALKAQCLAVDANArvdnpmadlqlvsddlgeLQRQAaeFTPNKDKAAIGENILGLRLLCLYGLK 160
Cdd:TIGR01703  76 EDRIVEYIEDAIKLREKLKKKCRLADSNS------------------LLIQS--FALNGDKSHVNDDVNSLRDLLLYGIK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  161 GAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:TIGR01703 136 GIAAYLYHARELGYDDEEIYAFLEEALASTLTNVFDADELIDLALEVGKMNLEAMKLLDKANTETYGLPEPTEVNIGTTE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:TIGR01703 216 GKAILVSGHDLKDLEELLEQTEGTGINVYTHGEMLPAHGYPELKKYPHLAGNYGGAWQDQQREFAEFPGPILMTSNCIIP 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  321 PTVgAYDDRIWTRSIVGWPGVRHLDGEDFSAVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIF 400
Cdd:TIGR01703 296 PRK-SYKDRIFTTGIVGWPGVKHIENYDFSPVIEKALELPGFPKELEEGTITTGFGHHTILALADKIVELVKEGKIRHFF 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  401 LLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVN 480
Cdd:TIGR01703 375 LVGGCDGPNPERNYYTEFARKLPKDAIILTLACGKYRFNKLDLGDIEGIPRLLDLGQCNDAYSAIEIALKLAEVFGCDVN 454
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446380986  481 DLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLL 548
Cdd:TIGR01703 455 ELPLSIVLSWYEQKAIAILLALLYLGVKNIYIGPTLPGFLTPNVFKILVDNFDLRLIGEPEDDLRAIL 522
HCP cd01914
Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in ...
1-548 0e+00

Hybrid cluster protein (HCP), formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. HCP has three structural domains, an N-terminal alpha-helical domain, and two similar domains comprising a central beta-sheet flanked by alpha-helices. HCP contains two iron-sulfur clusters, one of which is a [Fe4-S4] cubane cluster similar to that of carbon monoxide dehydrogenase (CODH). The second cluster, referred to as the hybrid cluster, is a hybrid [Fe4-S2-O2] center located at the interface of the three domains. Although the hybrid cluster is buried within the protein, it is accessible through a large hydrophobic cavity.


Pssm-ID: 238895  Cd Length: 423  Bit Score: 732.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTIRtpaGNGCSYAqGMCGKTAETSDLQDlliatlqglsawavkareygiinhdvdsfapraffstltnvnfd 80
Cdd:cd01914    1 MFCYQCEQTAK---GTGCTVR-GVCGKDPEVANLQD-------------------------------------------- 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  81 spriigyareaialrealkaqclavdanarvdnpmadlqlvsddlgelqrqaaeftpnkdkaaigenilglrllclYGLK 160
Cdd:cd01914   33 ----------------------------------------------------------------------------YGLK 36
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 161 GAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:cd01914   37 GIAAYAEHARVLGYDDEEIYAFIEKALASLLDNPLDADELLALALETGRMNLKVMELLDKANTETYGHPEPTEVNIGVRA 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:cd01914  117 GKGILVSGHDLKDLEELLEQTEGTGVDVYTHGEMLPAHGYPELKKYPHLVGNYGGAWQNQQKEFARFPGPILMTTNCIIP 196
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 321 PTvGAYDDRIWTRSIVGWPGVRHLDGEDFSAVIAQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIF 400
Cdd:cd01914  197 PR-ESYKDRIFTTGIVGWPGVKHIEGKDFSEVIEKAKELPGFPEEEESGTITTGFAHNQVLAVADKVVEAVKSGKIRHFF 275
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 401 LLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVN 480
Cdd:cd01914  276 VVGGCDGRHKGRNYYTEFAEKLPKDTVILTLGCGKYRFNKLDLGDIGGIPRLLDAGQCNDSYSAIVIALALAEAFGCDVN 355
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446380986 481 DLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLL 548
Cdd:cd01914  356 DLPLSLVLSWYEQKAVAVLLALLALGVKNIRLGPTLPAFLTPNVLKVLVENFGLKPIGTVEEDLKAIL 423
Prismane pfam03063
Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the ...
1-545 0e+00

Prismane/CO dehydrogenase family; This family includes both hybrid-cluster proteins and the beta chain of carbon monoxide dehydrogenase. The hybrid-cluster proteins contain two Fe/S centres - a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster. The physiological role of this protein is as yet unknown, although a role in nitrate/nitrite respiration has been suggested. The prismane protein from Escherichia coli was shown to contain hydroxylamine reductase activity (NH2OH + 2e + 2 H+ -> NH3 + H2O). This activity is rather low. Hydroxylamine reductase activity was also found in CO-dehydrogenase in which the active site Ni was replaced by Fe. The CO dehydrogenase contains a Ni-3Fe-2S-3O centre.


Pssm-ID: 460790 [Multi-domain]  Cd Length: 539  Bit Score: 577.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986    1 MFCVQCEqtirtpaGNGCSYAQ---GMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINHDvdsfaprAFFSTLTNV 77
Cdd:pfam03063   1 MFCRQCE-------MGPCRITPkprGVCGKTADTIVARNLLRYVAAGAAAHSDHARELGLTLKE-------ALFGTLTNY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   78 NFDSPRIIGYAREAIALREALKaqclavdanarvdnpmadlqlvsdDLGELQRQAAEFTPNkDKAAIGENILGLRLLCLY 157
Cdd:pfam03063  67 NIDDERKLKRIAEALGIRTELK------------------------DIEELAAEVADVGLE-DFYGKNEDIRSLRELAPY 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  158 GLKGAAAymEHAHVLGQYDNDIYAQYHKIMAWLGTWPADmnaLLECSMEIGQMNFKVMSILDAGETGKYGHPTP--TQVN 235
Cdd:pfam03063 122 GRKGLWA--EHAIVPGGIDREVFEFMHRTLTGLDSDPLD---LLLLALRCGLADLGGMELLDEANDILFGTPEPvlTEVN 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  236 --VKATAGKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELR-KFKHLVGNYGSGWQNQQVEFARFPGPIV 312
Cdd:pfam03063 197 lgVLDKDYVNILVSGHDPKDLEMLLEQTEGTGINVYAHGEMLPGHCCPGLKlKYRHGVGNYGNAWQQELAEFTGFPDAIV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  313 MTSNCIIDP---TVGAYDDRIWTRSIVGW-PGVRHLD------GEDFSAVIAQAQQMAGFP---YSEIPHLITVGFG--- 376
Cdd:pfam03063 277 VDTNCIMPPlasVASCYHTRLITTSPVGKiPGATHIEfdeekaDKDASEIIEKAIEAFKFReieKVEIPGEKVGGVAgfs 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  377 ----RQTLLGAADTLIDLVSREKLRHIFLLGGCDGARGERHYFTDFATSV-PDDCLILTLACGKYRFNKLEFGDIE---- 447
Cdd:pfam03063 357 teaiHEAVLGSADPLIDAIKSGAIRGFVLVVGCDNAKPGRDYYTELAKELiPKDILVLTTGCAKYRFNKLGLGDIEaael 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  448 ---GLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPL-SLVLSWFEQKAIVILLTLLSLGVkNIVTGPTAPGFLTPD 523
Cdd:pfam03063 437 agdGLPPVLDMGQCNDNYRAIVIALALAEALGVDINDLPLaSSAPEWYEQKAVAIGLTLLALGI-NIHLGPTPPAFGSPN 515
                         570       580
                  ....*....|....*....|....
gi 446380986  524 LLAVLNEKF--GLRSITTVEEDMK 545
Cdd:pfam03063 516 VLKVLTENFedLIGGIFTVEEDPK 539
PRK12310 PRK12310
hydroxylamine reductase; Provisional
1-550 0e+00

hydroxylamine reductase; Provisional


Pssm-ID: 183427  Cd Length: 433  Bit Score: 558.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTirtpAGNGCSYAqGMCGKTAETSDLQDLLIATLQGLSAWAVKAREYGIINHDVDSFAPRAFFSTLTNVNFD 80
Cdd:PRK12310   5 MFCYQCEQT----ATGGCTVM-GVCGKDETLASLQDTLIFGLKGIAAYRYHARELGYTDPEVDAFLAEALYSTLTNVNFD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  81 SPRIIGYAreaialrealkaqclavdanarvdnpmadlqlvsddlgelqrqaaeftpnkdkaaigenilglrllclyglk 160
Cdd:PRK12310  80 LQEHIDLA------------------------------------------------------------------------ 87
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 161 gaaaymehahvlgqydndiyaqyhkimawlgtwpadmnallecsMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATA 240
Cdd:PRK12310  88 --------------------------------------------LKVGKANLKVMELLDKAHTETFGEPEPVEVTQGTVE 123
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 241 GKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIID 320
Cdd:PRK12310 124 GKAILVTGHNLKALEELLKQTEGKGINVYTHSEMLPAHGYPELKKYKHLKGNIGKAWYDQRKLFEKFPGAILGTTNCVMP 203
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 321 PTvGAYDDRIWTRSIVGWPGVRHLDGEDFSAVIAQAQQMAGFPYSEIPHLITvGFGRQTLLGAADTLIDLVSREKLRHIF 400
Cdd:PRK12310 204 PK-GSYADRMFTYGIAGLEGVQHIENDDFTPLIEKALELPELEMESDETLVT-GFHHTTVLSLAPKIIEAVKEGKIRRFF 281
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 401 LLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEG--LPRLVDAGQCNDAYSAIILAVTLAEKLGCG 478
Cdd:PRK12310 282 VIAGCDAPGKGREYYRELATSLPKDTVILTLSCGKFRFNDLDYGTIEGteIPRYIDLGQCNDSISAVKIALALADAFGCE 361
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446380986 479 VNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLLSA 550
Cdd:PRK12310 362 VNDLPVSIVLSWMEQKAVAILLGLLSLGIKNIYIGPKLPEFLNPGVLEVLQENFNLKLISDPEEDLKKMLGK 433
Hcp COG1151
Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion];
1-548 1.98e-173

Hydroxylamine reductase (hybrid-cluster protein) [Energy production and conversion];


Pssm-ID: 440765  Cd Length: 613  Bit Score: 503.58  E-value: 1.98e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986   1 MFCVQCEQTirtpagnGCSY----AQGMCGKTAETSDLQDLLIATLQGLSAWAVKARE-------------YGIINHDVD 63
Cdd:COG1151   38 MCCRQCEQG-------PCRItpktPRGVCGKTADTIVARNLLRYVAKGAAAHADHAREvaltlkaaaegadYEIKDEEKL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986  64 SFAPRAFFSTltnvnfdsPRIIGYAREAIALREALKAQClavdanARVDNPMADLqlvsddlgeLQRQAAEftpnkdkaa 143
Cdd:COG1151  111 RFVAEALGIT--------TEGKDLIEIALELADALLEDF------GKAGGEPATW---------LEAKAPE--------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 144 igENILGLRLLclyglkgaaaymehahvlGQYDNDIYAQYHKIMAWLGT-WPADMNALLECSMEIGQMNFKVMSILDAGE 222
Cdd:COG1151  159 --ERIESWREL------------------GIEPRGIDREIVEALARTHTgVDLDPVNLLLLALRTGLADWGGMALLDEAN 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 223 TGKYGHPTPTQVN----VKATAGKCILISGHDLK----------DLYNLLEQTEGTGVNVY----THGEMLPAHGYPElR 284
Cdd:COG1151  219 DILFGTPEPTEVEvnlgVLKEDGVNILVHGHDPKlseaiveaarDLEELAKQTGAKGINVYgiccTGGEMLPRHGYPE-K 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 285 KFKHLVGNYGSGwqnqqvEFARFPGPI---VMTSNCIIDP----TVGAYDDRIWTRSIVGWPGVRHLDG------EDFSA 351
Cdd:COG1151  298 KYVHLAGNYGSA------EFAIFTGAIdamVVDTNCIMPPlasvAECYYTDRITTTGVVGIPGAEHIEFdeegalEDASE 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 352 VIAQAQQMAGFPYSEIPHL------ITVGFGRQTLLGA---ADTLIDLVSREKLRHIFLLGGCDGARGER--HYFTDFAT 420
Cdd:COG1151  372 IIEKAIENFKPREDEKVYIpqekgeIVVGFSHEAVLAAlgsADPLIDAIKSGKIRGFVLVVGCDGRKPGRdyNYYTLFKE 451
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 421 SVPDDCLILTLACGKYRFNKLEFGDIE----------------GLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPL 484
Cdd:COG1151  452 LIPNDVLVLTTGCAKYRLNKLGLGDIEaaelageglkevcealGIPPVLDMGQCNDNYRALVLALALAEALGVDINDLPL 531
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446380986 485 SLVL-SWFEQKAIVILLTLLSLGVKnIVTGPTAPGFLTPDLLAVLNEKF-GLRSIT-TVEEDMKQLL 548
Cdd:COG1151  532 AGSApEWYEQKAVAIGLYLLALGVK-IHLGPTPPAFGSPNVLKVLTEDFeDITGGTfTVEEDPKKAA 597
PRK05274 PRK05274
2-keto-3-deoxygluconate permease; Provisional
141-356 4.30e-17

2-keto-3-deoxygluconate permease; Provisional


Pssm-ID: 235384  Cd Length: 326  Bit Score: 82.25  E-value: 4.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 141 KAAIGENILGLRLLCLyGLKGAAAYMEHAHVLGQYDNDIYaqyHKIMAWLGTwPADMNALLECSMEIGQmnFKVMSILDA 220
Cdd:PRK05274  90 VGVIAGKFIGEEGIRL-GGFAGLSTLAIIAAMDNTNGGLY---AALMGQYGT-KEDAGAFVLMSLEDGP--FMTMLALGA 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 221 GETGKYGHPTPTQVNvkatagkCILISGHDLKDLYNLLEQTEGTGVNVythgeMLPAHGYPelrkfkhlvgnYGSGWQNQ 300
Cdd:PRK05274 163 AGLASFPPPALVGAV-------LPLLVGFILGNLDPELRQFLGKAVPV-----LIPFFAFA-----------LGNGIDLG 219
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446380986 301 QVEFARFPGPIVMTSNCIIDPTVGAYDDRIwtrsIVGWPGVRHLDGEDFS-------AVIAQA 356
Cdd:PRK05274 220 TIITAGLSGILLGVAVVAVTGIPLYLADRL----IGGGNGVAGAAAGSTAgnavatpAAVAAA 278
HCP_like cd00587
The HCP family of iron-sulfur proteins includes hybrid cluster protein (HCP), acetyl-CoA ...
399-548 4.98e-17

The HCP family of iron-sulfur proteins includes hybrid cluster protein (HCP), acetyl-CoA synthase (ACS), and carbon monoxide dehydrogenase (CODH), all of which contain [Fe4-S4] metal clusters at their active sites. These proteins have a conserved alpha-beta rossman fold domain. HCP, formerly known as prismane, is thought to play a role in nitrogen metabolism but its specific function is unknown. Acetyl-CoA synthase (ACS), is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide and CoA.


Pssm-ID: 238330 [Multi-domain]  Cd Length: 258  Bit Score: 81.10  E-value: 4.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 399 IFLLGGCDGARGERHYFTDFATSVPD-DCLILTLACGKYRFNKLEF----GDIEGLPRLVDAGQCNDAYSAIILAVTLAE 473
Cdd:cd00587   97 VALIVGCNNDKKQDKAYADIAKELMKrGVMVLATGCAAEALLKLGLedgaGILGGLPIVFDMGNCVDNSHAANLALKLAN 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 474 KLGC-GVNDLPLSLVLSW-FEQKAIVILLTLLSLGVKnIVTGPTAPGFLTPDLLAVL------NEKFGLRSITTVEEDMK 545
Cdd:cd00587  177 MFGGyDRSDLPAVASAPGaYSQKAAAIATGAVFLGVP-VHVGPPLPVDGSIPVWKVLtpeasdNEGGYFISVTDYQDIVQ 255

                 ...
gi 446380986 546 QLL 548
Cdd:cd00587  256 KAM 258
CODH cd01915
Carbon monoxide dehydrogenase (CODH) is found in acetogenic and methanogenic organisms and is ...
264-545 7.16e-09

Carbon monoxide dehydrogenase (CODH) is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA, respectively. CODH has two types of metal clusters, a cubane [Fe4-S4] center (B-cluster) similar to that of hybrid cluster protein (HCP) and a Ni-Fe-S center (C-cluster) where carbon monoxide oxidation occurs. Bifunctional CODH forms a heterotetramer with acetyl-CoA synthase (ACS) consisting of two CODH and two ACS subunits while monofunctional CODH forms a homodimer. Bifunctional CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP), while monofunctional CODH oxidizes carbon monoxide to carbon dioxide. CODH and ACS each have a metal cluster referred to as the C- and A-clusters, respectively.


Pssm-ID: 238896  Cd Length: 613  Bit Score: 58.43  E-value: 7.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 264 TGVNVY----THGEMLPAHGYPelrkfkhLVGNYGSgwqnqqVEFARFPGPI---VMTSNCIIdPTVGAYDDR-----IW 331
Cdd:cd01915  279 KGINVVgiccTGNELLMRHGVP-------LAGNWLS------QELAIATGAVdamVVDVQCIM-PSLPQYAECfhtklIT 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 332 TRSIVGWPGVRHLDGEDFSAViAQAQ---QMA----------GFPYSEIPHLITVGFGRQTLLGA----ADTLIDLVSRE 394
Cdd:cd01915  345 TSDVAKIPGAEHIDFDPEEAD-ESAKeiiRMAieafkrrkksKVYIPQHKSKAVVGFSTEAILDAlggsLKPLIDAIASG 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 395 KLRHIFLLGGCDGAR--GERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIE----------------GLPRLVDAG 456
Cdd:cd01915  424 NIKGVVGIVGCNNLKvqQDSSHVTLAKELIKRNVLVLATGCGAGALAKAGLMDPEaaelagdglkavckalGIPPVLHMG 503
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446380986 457 QCNDAYSAIILAVTLAEKLGCGVNDLPlsLVLS---WFEQKAIVILLTLLSLGVkNIVTGPTAPGFLTPDLLAVLNEkfG 533
Cdd:cd01915  504 SCVDNSRIVDLATALANELGVDIPDLP--LVASapeWMEEKAVAIGTWAVALGL-PTHVGPVPPVTGSDLVTKLLTE--D 578
                        330
                 ....*....|....*.
gi 446380986 534 LRSIT----TVEEDMK 545
Cdd:cd01915  579 LEDVTggkfIVETDPK 594
 
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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