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Conserved domains on  [gi|446599127|ref|WP_000676473|]
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MULTISPECIES: sirohydrochlorin chelatase [Bacillati]

Protein Classification

sirohydrochlorin chelatase( domain architecture ID 11450325)

sirohydrochlorin chelatase catalyzes the ferro-/cobalt- chelation of sirohydrochlorin to siroheme or cobalt-sirohydrochlorin

CATH:  3.40.50.1400|3.40.50.140
EC:  4.99.1.-
Gene Ontology:  GO:0016829
PubMed:  16469498|12196148
SCOP:  4002342

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-231 2.70e-64

Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ferrochelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 441741 [Multi-domain]  Cd Length: 230  Bit Score: 199.39  E-value: 2.70e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   1 MKGIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDI 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKEDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127  81 PFEIEQLQKKYPQITFSVVPPFSTHPHMVELVVKRIREAMPMQNSSILLVGRGSSDPQPIHELQQIGAAVERKLGmPVSC 160
Cdd:COG2138   83 PEALAEARARYPGVRIRLAPPLGPDPRLADLLAERLAEALARPDTAVVLVGRGSSDPDANADVAKLARLLAERLG-PVET 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446599127 161 SFLTkGTPSFAAEL-KAITSTASHVYVMPYLLFTGLLLQKIKLHTKKYNHVTtcNCLQFDTYMKLTLLERME 231
Cdd:COG2138  162 AFLG-TGPSLEEALeRLRALGARRVVVLPYFLFPGVLTDRIADQVAGADVVA--EPLGPHPELADLVLDRYR 230
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-231 2.70e-64

Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ferrochelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441741 [Multi-domain]  Cd Length: 230  Bit Score: 199.39  E-value: 2.70e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   1 MKGIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDI 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKEDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127  81 PFEIEQLQKKYPQITFSVVPPFSTHPHMVELVVKRIREAMPMQNSSILLVGRGSSDPQPIHELQQIGAAVERKLGmPVSC 160
Cdd:COG2138   83 PEALAEARARYPGVRIRLAPPLGPDPRLADLLAERLAEALARPDTAVVLVGRGSSDPDANADVAKLARLLAERLG-PVET 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446599127 161 SFLTkGTPSFAAEL-KAITSTASHVYVMPYLLFTGLLLQKIKLHTKKYNHVTtcNCLQFDTYMKLTLLERME 231
Cdd:COG2138  162 AFLG-TGPSLEEALeRLRALGARRVVVLPYFLFPGVLTDRIADQVAGADVVA--EPLGPHPELADLVLDRYR 230
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 9-114 1.37e-37

CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons and so may have a related function. Some CbiX proteins contain a striking histidine-rich region at their C-terminus, which suggests that it might be involved in metal chelation.


Pssm-ID: 396469 [Multi-domain]  Cd Length: 106  Bit Score: 126.97  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127    9 HGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDIPFEIEQLQ 88
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLPVEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPEELAAAK 80

                          90       100
                  ....*....|....*....|....*.
gi 446599127   89 KKYPQITFSVVPPFSTHPHMVELVVK 114
Cdd:pfam01903  81 AAHPDIEIRYAPPLGPHPLLAELLRE 106
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 3-102 5.58e-35

Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), N-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both are found in a wide range of bacteria. This subgroup also contains single domain proteins from archaea and bacteria which may represent the ancestral form of class II chelatases before domain duplication occurred.


Pssm-ID: 239509 [Multi-domain]  Cd Length: 101  Bit Score: 120.37  E-value: 5.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   3 GIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDIPF 82
Cdd:cd03416    1 ALLLVGHGSRDPRAAEALEALAERLRERLPGDEVELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHVKEDIPA 80

                         90       100
                 ....*....|....*....|
gi 446599127  83 EIEQLQKKYPQITFSVVPPF 102
Cdd:cd03416   81 ALAAARARHPGVRIRYAPPL 100
PLN02757 PLN02757
sirohydrochlorine ferrochelatase
 3-120 8.01e-21

sirohydrochlorine ferrochelatase


Pssm-ID: 215403 [Multi-domain]  Cd Length: 154  Bit Score: 85.18  E-value: 8.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   3 GIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDIPF 82
Cdd:PLN02757  15 GVVIVDHGSRRKESNLMLEEFVAMYKQKTGHPIVEPAHMELAEPSIKDAFGRCVEQGASRVIVSPFFLSPGRHWQEDIPA 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446599127  83 EIEQLQKKYPQITFSVVPPFSTHPHMVELVVKRIREAM 120
Cdd:PLN02757  95 LTAEAAKEHPGVKYLVTAPIGLHELMVDVVNDRIKYCL 132
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-231 2.70e-64

Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ferrochelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441741 [Multi-domain]  Cd Length: 230  Bit Score: 199.39  E-value: 2.70e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   1 MKGIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDI 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKEDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127  81 PFEIEQLQKKYPQITFSVVPPFSTHPHMVELVVKRIREAMPMQNSSILLVGRGSSDPQPIHELQQIGAAVERKLGmPVSC 160
Cdd:COG2138   83 PEALAEARARYPGVRIRLAPPLGPDPRLADLLAERLAEALARPDTAVVLVGRGSSDPDANADVAKLARLLAERLG-PVET 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446599127 161 SFLTkGTPSFAAEL-KAITSTASHVYVMPYLLFTGLLLQKIKLHTKKYNHVTtcNCLQFDTYMKLTLLERME 231
Cdd:COG2138  162 AFLG-TGPSLEEALeRLRALGARRVVVLPYFLFPGVLTDRIADQVAGADVVA--EPLGPHPELADLVLDRYR 230
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 9-114 1.37e-37

CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons and so may have a related function. Some CbiX proteins contain a striking histidine-rich region at their C-terminus, which suggests that it might be involved in metal chelation.


Pssm-ID: 396469 [Multi-domain]  Cd Length: 106  Bit Score: 126.97  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127    9 HGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDIPFEIEQLQ 88
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLPVEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPEELAAAK 80

                          90       100
                  ....*....|....*....|....*.
gi 446599127   89 KKYPQITFSVVPPFSTHPHMVELVVK 114
Cdd:pfam01903  81 AAHPDIEIRYAPPLGPHPLLAELLRE 106
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 3-102 5.58e-35

Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), N-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both are found in a wide range of bacteria. This subgroup also contains single domain proteins from archaea and bacteria which may represent the ancestral form of class II chelatases before domain duplication occurred.


Pssm-ID: 239509 [Multi-domain]  Cd Length: 101  Bit Score: 120.37  E-value: 5.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   3 GIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDIPF 82
Cdd:cd03416    1 ALLLVGHGSRDPRAAEALEALAERLRERLPGDEVELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHVKEDIPA 80

                         90       100
                 ....*....|....*....|
gi 446599127  83 EIEQLQKKYPQITFSVVPPF 102
Cdd:cd03416   81 ALAAARARHPGVRIRYAPPL 100
CbiX_SirB_C cd03414
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 125-234 1.26e-30

Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), C-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both CbiX and SirB are found in a wide range of bacteria.


Pssm-ID: 239507 [Multi-domain]  Cd Length: 117  Bit Score: 109.62  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127 125 SSILLVGRGSSDPQPIHELQQIGAAVERKLG-MPVSCSFLTKGTPSFAAELK-AITSTASHVYVMPYLLFTGLLLQKIKL 202
Cdd:cd03414    1 TAVVLVGRGSSDPDANADVAKIARLLEEGTGfARVETAFAAATRPSLPEALErLRALGARRVVVLPYLLFTGVLMDRIEE 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446599127 203 HTKKYN-----HVTTCNCLQFDTYMKLTLLERMEECI 234
Cdd:cd03414   81 QVAELAaepgiEFVLAPPLGPHPELAEALLERVREAL 117
PLN02757 PLN02757
sirohydrochlorine ferrochelatase
 3-120 8.01e-21

sirohydrochlorine ferrochelatase


Pssm-ID: 215403 [Multi-domain]  Cd Length: 154  Bit Score: 85.18  E-value: 8.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   3 GIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDIPF 82
Cdd:PLN02757  15 GVVIVDHGSRRKESNLMLEEFVAMYKQKTGHPIVEPAHMELAEPSIKDAFGRCVEQGASRVIVSPFFLSPGRHWQEDIPA 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446599127  83 EIEQLQKKYPQITFSVVPPFSTHPHMVELVVKRIREAM 120
Cdd:PLN02757  95 LTAEAAKEHPGVKYLVTAPIGLHELMVDVVNDRIKYCL 132
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
1-119 3.62e-20

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 82.62  E-value: 3.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   1 MKGIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDI 80
Cdd:PRK00923   1 MLGLLLVGHGSRLPYNKEVVTKIAEKIKEKHPFYIVEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGVHTKRDI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446599127  81 PFE--IEQLQKKYPQITFSVVP-----PFSTHPHMVELVVKRIREA 119
Cdd:PRK00923  81 PRIlgLDEGEKEEIEEDGKDVEivyaePLGADERIADIVLKRANEA 126
CbiX_SirB_C cd03414
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 3-120 6.40e-11

Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), C-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both CbiX and SirB are found in a wide range of bacteria.


Pssm-ID: 239507 [Multi-domain]  Cd Length: 117  Bit Score: 58.00  E-value: 6.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   3 GIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRdIPF 82
Cdd:cd03414    2 AVVLVGRGSSDPDANADVAKIARLLEEGTGFARVETAFAAATRPSLPEALERLRALGARRVVVLPYLLFTGVLMDR-IEE 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446599127  83 EIEQLQKKyPQITFSVVPPFSTHPHMVELVVKRIREAM 120
Cdd:cd03414   81 QVAELAAE-PGIEFVLAPPLGPHPELAEALLERVREAL 117
Chelatase_Class_II cd03409
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze ...
 3-90 6.20e-08

Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze the insertion of metal into protoporphyrin rings. This family includes protoporphyrin IX ferrochelatase (HemH), sirohydrochlorin ferrochelatase (SirB) and the cobaltochelatases, CbiK and CbiX. HemH and SirB are involved in heme and siroheme biosynthesis, respectively, while the cobaltochelatases are associated with cobalamin biosynthesis. Excluded from this family are the ATP-dependent heterotrimeric chelatases (class I) and the multifunctional homodimeric enzymes with dehydrogenase and chelatase activities (class III).


Pssm-ID: 239503 [Multi-domain]  Cd Length: 101  Bit Score: 49.29  E-value: 6.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   3 GIVYVGHGSRLQEGNEQFI-QFIQSVMKERNERIQKIAFLELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDIP 81
Cdd:cd03409    1 GLLVVGHGSPYKDPYKKDIeAQAHNLAESLPDFPYYVGFQSGLGPDTEEAIRELAEEGYQRVVIVPLAPVSGDEVFYDID 80


                 ....*....
gi 446599127  82 FEIEQLQKK 90
Cdd:cd03409   81 SEIGLVRKQ 89
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 122-194 1.64e-07

Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ferrochelatase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441741 [Multi-domain]  Cd Length: 230  Bit Score: 50.32  E-value: 1.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446599127 122 MQNSSILLVGRGSSDPQPIHELQQIGAAVERKL-GMPVSCSFLTKGTPSFAAELKAITST-ASHVYVMPYLLFTG 194
Cdd:COG2138    1 MMKTALLLVAHGSRDPEGAEEFEALAARLRARLpGLPVELAFLELAEPSLEEALDALVAQgATRIVVVPLFLAAG 75
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 126-194 8.78e-07

Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), N-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both are found in a wide range of bacteria. This subgroup also contains single domain proteins from archaea and bacteria which may represent the ancestral form of class II chelatases before domain duplication occurred.


Pssm-ID: 239509 [Multi-domain]  Cd Length: 101  Bit Score: 46.03  E-value: 8.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446599127 126 SILLVGRGSSDPQPIHELQQIGAAVERKL-GMPVSCSFLTKGTPSFAAELKA-ITSTASHVYVMPYLLFTG 194
Cdd:cd03416    1 ALLLVGHGSRDPRAAEALEALAERLRERLpGDEVELAFLELAEPSLAEALDElAAQGATRIVVVPLFLLAG 71
PRK05782 PRK05782
bifunctional sirohydrochlorin cobalt chelatase/precorrin-8X methylmutase; Validated
 1-142 1.11e-05

bifunctional sirohydrochlorin cobalt chelatase/precorrin-8X methylmutase; Validated


Pssm-ID: 235605 [Multi-domain]  Cd Length: 335  Bit Score: 45.57  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   1 MKGIVYVGHGSRlqegNEQFIQFIQSVMKERNERIQKIAFL---ELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYK 77
Cdd:PRK05782   6 NTAIILIGHGSR----RETFNSDMEGMANYLKEKLGVPIYLtynEFAEPNWRSLLNEIIKEGYRRVIIALAFLGRGNHVF 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446599127  78 RDI-------PFEIEQLQKKY-PQITFSVVPPFSTHPHMVELVVKRIREAMPMQNSsillvGRGSSDPQPIHE 142
Cdd:PRK05782  82 RDImgelgvqRLNSWEVSKISgKEVEFYVTEPLSDSPLVGLALYYRLARALDALPT-----LEYTEDPEEIEE 149
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 132-199 5.32e-05

CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons and so may have a related function. Some CbiX proteins contain a striking histidine-rich region at their C-terminus, which suggests that it might be involved in metal chelation.


Pssm-ID: 396469 [Multi-domain]  Cd Length: 106  Bit Score: 41.07  E-value: 5.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127  132 RGSSDPQPIHELQQIGAAVERKLG-MPVSCSFLTKGTPSFAAELKA-ITSTASHVYVMPYLLFTGLLLQK 199
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPfLPVEVAFLELAEPSLEEALRElVAQGVRRIVVVPLFLFAGGHVKR 70
HemH COG0276
Protoheme ferro-lyase (ferrochelatase) [Coenzyme transport and metabolism]; Protoheme ...
 7-120 5.35e-05

Protoheme ferro-lyase (ferrochelatase) [Coenzyme transport and metabolism]; Protoheme ferro-lyase (ferrochelatase) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440045 [Multi-domain]  Cd Length: 322  Bit Score: 43.17  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   7 VGHGSRLQEGNEQFIQFIQSVMKERNERIQ-KIAFLeLTTPTISDAVTETIIEGVTEIMIVPvlLFAaaHYK-------R 78
Cdd:COG0276   65 IGGGSPLNVITRRQAAALQAELAERGDDVPvYLAMR-YGNPSIEDALEELKADGVDRILVLP--LYP--QYSasttgsyF 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446599127  79 DipfEIEQLQKKY-PQITFSVVPPFSTHPHMVELVVKRIREAM 120
Cdd:COG0276  140 D---DVARALKKLrWQPEIRFIRSYYDHPGYIEALAESIREAL 179
hemH PRK00035
ferrochelatase; Reviewed
 44-120 2.31e-04

ferrochelatase; Reviewed


Pssm-ID: 234585 [Multi-domain]  Cd Length: 333  Bit Score: 41.32  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127  44 TTPTISDAVTETIIEGVTEIMIVPvlLFA------AAHYKRDIpfeIEQLQKKYPQITFSVVPPFSTHPHMVELVVKRIR 117
Cdd:PRK00035 103 WNPSIEEALEALKADGVDRIVVLP--LYPqysystTASYFEDL---ARALAKLRLQPEIRFIRSYYDHPGYIEALAESIR 177


                 ...
gi 446599127 118 EAM 120
Cdd:PRK00035 178 EAL 180
CbiK_C cd03413
Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), C-terminal domain. CbiK is part of ...
 4-80 8.74e-04

Anaerobic cobalamin biosynthetic cobalt chelatase (CbiK), C-terminal domain. CbiK is part of the cobalt-early path for cobalamin biosynthesis. It catalyzes the insertion of cobalt into the oxidized form of precorrin-2, factor II (sirohydrochlorin), the second step of the anaerobic branch of vitamin B12 biosynthesis. CbiK belongs to the class II family of chelatases, and is a homomeric enzyme that does not require ATP for its enzymatic activity.


Pssm-ID: 239506 [Multi-domain]  Cd Length: 103  Bit Score: 37.61  E-value: 8.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446599127   4 IVYVGHGSRlQEGNEQFIQfIQSVMKERNERIQKIAFLElTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDI 80
Cdd:cd03413    3 VVFMGHGTD-HPSNAVYAA-LEYVLREEDPANVFVGTVE-GYPGLDDVLAKLKKAGIKKVTLMPLMLVAGDHAHNDM 76
Ferrochelatase pfam00762
Ferrochelatase;
46-119 1.10e-03

Ferrochelatase;


Pssm-ID: 459929 [Multi-domain]  Cd Length: 315  Bit Score: 39.43  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   46 PTISDAVTETIIEGVTEIMIVPvlLFAaaHYK--------RDIpfeIEQLQKKYPQITFSVVPPFSTHPHMVELVVKRIR 117
Cdd:pfam00762  99 PSIEDALEELKADGVERIVVLP--LYP--QYSssttgsylDEL---ARALKKGRPAPELRFIRDYYDHPGYIEALAESIR 171


                  ..
gi 446599127  118 EA 119
Cdd:pfam00762 172 EA 173
PRK02395 PRK02395
hypothetical protein; Provisional
 3-119 1.69e-03

hypothetical protein; Provisional


Pssm-ID: 235034 [Multi-domain]  Cd Length: 279  Bit Score: 38.91  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   3 GIVYVGHGSRLQEGNEQFIQFIQSVMKERNERIQKIAFLELTTPTISDaVTEtIIEGvTEIMIVPvlLFAAA--HYKRDI 80
Cdd:PRK02395 137 ALAVVGHGTERNENSAKAIYYHADRLRERGRFAEVEALFLDEEPEVDD-WPD-LFEA-DDVVVVP--LFIADgfHTQEDI 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446599127  81 PfEIEQLQKKYpqITFSVVP------------PFSTHPHMVELVVKRIREA 119
Cdd:PRK02395 212 P-EDMGLTDDY--RTGYDVPtavdghriwyagAVGTEPLMADVILERAADA 259
CbiX_CbiC cd03415
Archaeal sirohydrochlorin cobalt chelatase (CbiX) single domain. Proteins in this subgroup ...
 4-80 5.30e-03

Archaeal sirohydrochlorin cobalt chelatase (CbiX) single domain. Proteins in this subgroup contain a single CbiX domain N-terminal to a precorrin-8X methylmutase (CbiC) domain. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, while CbiC catalyzes the conversion of cobalt-precorrin 8 to cobyrinic acid by methyl rearrangement. Both CbiX and CbiC are involved in vitamin B12 biosynthesis.


Pssm-ID: 239508  Cd Length: 125  Bit Score: 35.97  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446599127   4 IVYVGHGSRlqegNEQFIQFIQSVMKERNERIQKIAFL---ELTTPTISDAVTETIIEGVTEIMIVPVLLFAAAHYKRDI 80
Cdd:cd03415    3 IIIITHGSR----RNTFNEDMEEWAAYLERKLGVPVYLtynEYAEPNWRDLLNELLSEGYGHIIIALAFLGRGNHVARDI 78
 
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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