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Conserved domains on  [gi|446571535|ref|WP_000648881|]
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MULTISPECIES: sirohydrochlorin chelatase [Bacillus]

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 ...
 1-233 6.66e-65

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: 201.70  E-value: 6.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   1 MKAVLYICHGSRLKTAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDI 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKEDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535  81 PFELVKLKNQYPNVKVTYGNPFGVSETLIKSVYNgSGIEKEGKAEVTLLLVARGSSDPEVLQDIKWIASLFQaeEKIKKV 160
Cdd:COG2138   83 PEALAEARARYPGVRIRLAPPLGPDPRLADLLAE-RLAEALARPDTAVVLVGRGSSDPDANADVAKLARLLA--ERLGPV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446571535 161 EVCYLaAAEPKFERKLKEVVEREVENIVVLPYLLFTGLLMKHIEKEVRQYALeeikISPYLGKNEALQDMLIQ 233
Cdd:COG2138  160 ETAFL-GTGPSLEEALERLRALGARRVVVLPYFLFPGVLTDRIADQVAGADV----VAEPLGPHPELADLVLD 227
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-233 6.66e-65

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: 201.70  E-value: 6.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   1 MKAVLYICHGSRLKTAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDI 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKEDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535  81 PFELVKLKNQYPNVKVTYGNPFGVSETLIKSVYNgSGIEKEGKAEVTLLLVARGSSDPEVLQDIKWIASLFQaeEKIKKV 160
Cdd:COG2138   83 PEALAEARARYPGVRIRLAPPLGPDPRLADLLAE-RLAEALARPDTAVVLVGRGSSDPDANADVAKLARLLA--ERLGPV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446571535 161 EVCYLaAAEPKFERKLKEVVEREVENIVVLPYLLFTGLLMKHIEKEVRQYALeeikISPYLGKNEALQDMLIQ 233
Cdd:COG2138  160 ETAFL-GTGPSLEEALERLRALGARRVVVLPYFLFPGVLTDRIADQVAGADV----VAEPLGPHPELADLVLD 227
CbiX_SirB_C cd03414
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 126-239 1.90e-38

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: 130.03  E-value: 1.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535 126 VTLLLVARGSSDPEVLQDIKWIASLFQAEEKIKKVEVCYLAAAEPKFERKLKEVVEREVENIVVLPYLLFTGLLMKHIEK 205
Cdd:cd03414    1 TAVVLVGRGSSDPDANADVAKIARLLEEGTGFARVETAFAAATRPSLPEALERLRALGARRVVVLPYLLFTGVLMDRIEE 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446571535 206 EVRQYALE---EIKISPYLGKNEALQDMLIQKTTELL 239
Cdd:cd03414   81 QVAELAAEpgiEFVLAPPLGPHPELAEALLERVREAL 117
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 9-114 1.23e-32

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: 115.03  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535    9 HGSRLKTAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDIPFELVKLK 88
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLPVEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPEELAAAK 80

                          90       100
                  ....*....|....*....|....*.
gi 446571535   89 NQYPNVKVTYGNPFGVSETLIKSVYN 114
Cdd:pfam01903  81 AAHPDIEIRYAPPLGPHPLLAELLRE 106
F430_CfbA NF033198
sirohydrochlorin nickelochelatase; Members of this family are sirohydrochlorin ...
 3-109 5.84e-16

sirohydrochlorin nickelochelatase; Members of this family are sirohydrochlorin nickelochelatase, involving in synthesizing coenzyme F430, used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) sirohydrochlorin cobaltochelatase , involved in cobalamin biosynthesis. Some members of this family are double in length because of a duplication.


Pssm-ID: 467993  Cd Length: 124  Bit Score: 71.75  E-value: 5.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   3 AVLYICHGSRLKTAKEeaiqFITSCMSRIEAN----IQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFlLAAG-HVK 77
Cdd:NF033198   1 GILLVGHGSRLPYNKE----VIESIAEMIKEKgdyyIVEVGFMELNEPTIPEALDKLAGEGVDKIIVVPVF-LAHGvHTT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446571535  78 KDIPFEL----------VKLKNQypNVKVTYGNPFGVSETLI 109
Cdd:NF033198  76 EDIPEILgldegtdegtIEFDGK--EVEIVYAEPIGADPRIA 115
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
1-113 1.07e-15

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 71.06  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   1 MKAVLYICHGSRLKTAKEEAIQfITSCMSRIEA-NIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKD 79
Cdd:PRK00923   1 MLGLLLVGHGSRLPYNKEVVTK-IAEKIKEKHPfYIVEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGVHTKRD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446571535  80 IPfELVKLKNQYPN--------VKVTYGNPFGVSETLIKSVY 113
Cdd:PRK00923  80 IP-RILGLDEGEKEeieedgkdVEIVYAEPLGADERIADIVL 120
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-233 6.66e-65

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: 201.70  E-value: 6.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   1 MKAVLYICHGSRLKTAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDI 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKEDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535  81 PFELVKLKNQYPNVKVTYGNPFGVSETLIKSVYNgSGIEKEGKAEVTLLLVARGSSDPEVLQDIKWIASLFQaeEKIKKV 160
Cdd:COG2138   83 PEALAEARARYPGVRIRLAPPLGPDPRLADLLAE-RLAEALARPDTAVVLVGRGSSDPDANADVAKLARLLA--ERLGPV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446571535 161 EVCYLaAAEPKFERKLKEVVEREVENIVVLPYLLFTGLLMKHIEKEVRQYALeeikISPYLGKNEALQDMLIQ 233
Cdd:COG2138  160 ETAFL-GTGPSLEEALERLRALGARRVVVLPYFLFPGVLTDRIADQVAGADV----VAEPLGPHPELADLVLD 227
CbiX_SirB_C cd03414
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 126-239 1.90e-38

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: 130.03  E-value: 1.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535 126 VTLLLVARGSSDPEVLQDIKWIASLFQAEEKIKKVEVCYLAAAEPKFERKLKEVVEREVENIVVLPYLLFTGLLMKHIEK 205
Cdd:cd03414    1 TAVVLVGRGSSDPDANADVAKIARLLEEGTGFARVETAFAAATRPSLPEALERLRALGARRVVVLPYLLFTGVLMDRIEE 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446571535 206 EVRQYALE---EIKISPYLGKNEALQDMLIQKTTELL 239
Cdd:cd03414   81 QVAELAAEpgiEFVLAPPLGPHPELAEALLERVREAL 117
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 3-103 2.56e-34

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: 118.83  E-value: 2.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   3 AVLYICHGSRLKTAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDIPF 82
Cdd:cd03416    1 ALLLVGHGSRDPRAAEALEALAERLRERLPGDEVELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHVKEDIPA 80

                         90       100
                 ....*....|....*....|.
gi 446571535  83 ELVKLKNQYPNVKVTYGNPFG 103
Cdd:cd03416   81 ALAAARARHPGVRIRYAPPLG 101
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 9-114 1.23e-32

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: 115.03  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535    9 HGSRLKTAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDIPFELVKLK 88
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLPVEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPEELAAAK 80

                          90       100
                  ....*....|....*....|....*.
gi 446571535   89 NQYPNVKVTYGNPFGVSETLIKSVYN 114
Cdd:pfam01903  81 AAHPDIEIRYAPPLGPHPLLAELLRE 106
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 133-233 1.89e-22

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: 88.45  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535  133 RGSSDPEVLQDIKWIASLFQAEEKIKKVEVCYLAAAEPKFERKLKEVVEREVENIVVLPYLLFTGLLMKH-IEKEVRQYA 211
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLPVEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRdIPEELAAAK 80

                          90       100
                  ....*....|....*....|....*.
gi 446571535  212 LE----EIKISPYLGKNEALQDMLIQ 233
Cdd:pfam01903  81 AAhpdiEIRYAPPLGPHPLLAELLRE 106
F430_CfbA NF033198
sirohydrochlorin nickelochelatase; Members of this family are sirohydrochlorin ...
 3-109 5.84e-16

sirohydrochlorin nickelochelatase; Members of this family are sirohydrochlorin nickelochelatase, involving in synthesizing coenzyme F430, used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) sirohydrochlorin cobaltochelatase , involved in cobalamin biosynthesis. Some members of this family are double in length because of a duplication.


Pssm-ID: 467993  Cd Length: 124  Bit Score: 71.75  E-value: 5.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   3 AVLYICHGSRLKTAKEeaiqFITSCMSRIEAN----IQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFlLAAG-HVK 77
Cdd:NF033198   1 GILLVGHGSRLPYNKE----VIESIAEMIKEKgdyyIVEVGFMELNEPTIPEALDKLAGEGVDKIIVVPVF-LAHGvHTT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446571535  78 KDIPFEL----------VKLKNQypNVKVTYGNPFGVSETLI 109
Cdd:NF033198  76 EDIPEILgldegtdegtIEFDGK--EVEIVYAEPIGADPRIA 115
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
1-113 1.07e-15

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 71.06  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   1 MKAVLYICHGSRLKTAKEEAIQfITSCMSRIEA-NIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKD 79
Cdd:PRK00923   1 MLGLLLVGHGSRLPYNKEVVTK-IAEKIKEKHPfYIVEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGVHTKRD 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446571535  80 IPfELVKLKNQYPN--------VKVTYGNPFGVSETLIKSVY 113
Cdd:PRK00923  80 IP-RILGLDEGEKEeieedgkdVEIVYAEPLGADERIADIVL 120
PLN02757 PLN02757
sirohydrochlorine ferrochelatase
 3-109 4.03e-14

sirohydrochlorine ferrochelatase


Pssm-ID: 215403 [Multi-domain]  Cd Length: 154  Bit Score: 67.85  E-value: 4.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   3 AVLYICHGSRLKTAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDIPF 82
Cdd:PLN02757  15 GVVIVDHGSRRKESNLMLEEFVAMYKQKTGHPIVEPAHMELAEPSIKDAFGRCVEQGASRVIVSPFFLSPGRHWQEDIPA 94

                         90       100
                 ....*....|....*....|....*..
gi 446571535  83 ELVKLKNQYPNVKVTYGNPFGVSETLI 109
Cdd:PLN02757  95 LTAEAAKEHPGVKYLVTAPIGLHELMV 121
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 128-222 9.57e-09

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: 51.80  E-value: 9.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535 128 LLLVARGSSDPEVLQDIKWIASLFQAEEKIKKVEVCYLAAAEPKFERKLKEVVEREVENIVVLPYLLFTGLLMKH-IEKE 206
Cdd:cd03416    2 LLLVGHGSRDPRAAEALEALAERLRERLPGDEVELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHVKEdIPAA 81

                         90       100
                 ....*....|....*....|
gi 446571535 207 VRQYALE----EIKISPYLG 222
Cdd:cd03416   82 LAAARARhpgvRIRYAPPLG 101
Chelatase_Class_II cd03409
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze ...
 3-95 2.54e-06

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: 45.06  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535   3 AVLYICHGSRLK-TAKEEAIQFITSCMSRIEANIQEVCFLELANPSIEDGFRTCVKRGATEIIAIPVFLLAAGHVKKDIP 81
Cdd:cd03409    1 GLLVVGHGSPYKdPYKKDIEAQAHNLAESLPDFPYYVGFQSGLGPDTEEAIRELAEEGYQRVVIVPLAPVSGDEVFYDID 80

                         90
                 ....*....|....
gi 446571535  82 FElvkLKNQYPNVK 95
Cdd:cd03409   81 SE---IGLVRKQVG 91
Chelatase_Class_II cd03409
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze ...
 128-217 4.01e-06

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: 44.29  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535 128 LLLVARGSSDPEVL-QDIKWIASLFQAEEKIKKVEVCYLAAAEPKFERKLKEVVEREVENIVVLPYLLFTGL-LMKHIEK 205
Cdd:cd03409    2 LLVVGHGSPYKDPYkKDIEAQAHNLAESLPDFPYYVGFQSGLGPDTEEAIRELAEEGYQRVVIVPLAPVSGDeVFYDIDS 81

                         90
                 ....*....|..
gi 446571535 206 EVRQYALEEIKI 217
Cdd:cd03409   82 EIGLVRKQVGEP 93
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
128-207 8.92e-04

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 38.32  E-value: 8.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446571535 128 LLLVARGSSDPEVLQDIKWIAslfqaeEKIKK------VEVCYLAAAEPKFERKLKEVVEREVENIVVLPYLLFTGLlmk 201
Cdd:PRK00923   4 LLLVGHGSRLPYNKEVVTKIA------EKIKEkhpfyiVEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGV--- 74


                 ....*.
gi 446571535 202 HIEKEV 207
Cdd:PRK00923  75 HTKRDI 80
 
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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