NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|896153278|ref|WP_049169883|]
View 

MULTISPECIES: sirohydrochlorin chelatase [Corynebacterium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-244 5.04e-34

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: 122.35  E-value: 5.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   1 MTALILLAHGSRHSETKPVLEDVVALVREKMPLTRldapsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAF 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLP------VELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278  81 HSRVDVPEQVRLCDRH--GVDITVAEGLGLGDGTKRAVVKRIIEAAENasfswPVDALVM-GVGSSDEDANAAVHQFAAN 157
Cdd:COG2138   77 HVKEDIPEALAEARARypGVRIRLAPPLGPDPRLADLLAERLAEALAR-----PDTAVVLvGRGSSDPDANADVAKLARL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278 158 LGGMLpGHVSAAFVVGPEKIKGAdavaaAQERAAKRGRGLVVVPLFTAPGLLWDRVIDAgaadGAGQVAFGEPL--AELL 235
Cdd:COG2138  152 LAERL-GPVETAFLGTGPSLEEA-----LERLRALGARRVVVLPYFLFPGVLTDRIADQ----VAGADVVAEPLgpHPEL 221


                 ....*....
gi 896153278 236 APIVCCRWD 244
Cdd:COG2138  222 ADLVLDRYR 230
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-244 5.04e-34

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: 122.35  E-value: 5.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   1 MTALILLAHGSRHSETKPVLEDVVALVREKMPLTRldapsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAF 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLP------VELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278  81 HSRVDVPEQVRLCDRH--GVDITVAEGLGLGDGTKRAVVKRIIEAAENasfswPVDALVM-GVGSSDEDANAAVHQFAAN 157
Cdd:COG2138   77 HVKEDIPEALAEARARypGVRIRLAPPLGPDPRLADLLAERLAEALAR-----PDTAVVLvGRGSSDPDANADVAKLARL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278 158 LGGMLpGHVSAAFVVGPEKIKGAdavaaAQERAAKRGRGLVVVPLFTAPGLLWDRVIDAgaadGAGQVAFGEPL--AELL 235
Cdd:COG2138  152 LAERL-GPVETAFLGTGPSLEEA-----LERLRALGARRVVVLPYFLFPGVLTDRIADQ----VAGADVVAEPLgpHPEL 221


                 ....*....
gi 896153278 236 APIVCCRWD 244
Cdd:COG2138  222 ADLVLDRYR 230
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 3-107 1.43e-20

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: 83.39  E-value: 1.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   3 ALILLAHGSRHSETKPVLEDVVALVREKMPLTRldapsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAFHS 82
Cdd:cd03416    1 ALLLVGHGSRDPRAAEALEALAERLRERLPGDE------VELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHV 74

                         90       100
                 ....*....|....*....|....*..
gi 896153278  83 RVDVPEQVRLCDR--HGVDITVAEGLG 107
Cdd:cd03416   75 KEDIPAALAAARArhPGVRIRYAPPLG 101
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 9-107 6.88e-12

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: 60.33  E-value: 6.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278    9 HGSRHSETKPVLEDVVALVREKMPLTRldapsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAFHSRVDVPE 88
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLP------VEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPE 74

                          90       100
                  ....*....|....*....|.
gi 896153278   89 QVRLCDRH--GVDITVAEGLG 107
Cdd:pfam01903  75 ELAAAKAAhpDIEIRYAPPLG 95
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
1-123 7.16e-07

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 47.18  E-value: 7.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   1 MTALILLAHGSRHSETKPVLEDVVALVREKMPltrlDAPsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAF 80
Cdd:PRK00923   1 MLGLLLVGHGSRLPYNKEVVTKIAEKIKEKHP----FYI--VEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896153278  81 HSRVDVPEQVRL--CDRH-------GVDITVAEGLGLGDGTKRAVVKRIIEA 123
Cdd:PRK00923  75 HTKRDIPRILGLdeGEKEeieedgkDVEIVYAEPLGADERIADIVLKRANEA 126
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 1-244 5.04e-34

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: 122.35  E-value: 5.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   1 MTALILLAHGSRHSETKPVLEDVVALVREKMPLTRldapsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAF 80
Cdd:COG2138    3 KTALLLVAHGSRDPEGAEEFEALAARLRARLPGLP------VELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278  81 HSRVDVPEQVRLCDRH--GVDITVAEGLGLGDGTKRAVVKRIIEAAENasfswPVDALVM-GVGSSDEDANAAVHQFAAN 157
Cdd:COG2138   77 HVKEDIPEALAEARARypGVRIRLAPPLGPDPRLADLLAERLAEALAR-----PDTAVVLvGRGSSDPDANADVAKLARL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278 158 LGGMLpGHVSAAFVVGPEKIKGAdavaaAQERAAKRGRGLVVVPLFTAPGLLWDRVIDAgaadGAGQVAFGEPL--AELL 235
Cdd:COG2138  152 LAERL-GPVETAFLGTGPSLEEA-----LERLRALGARRVVVLPYFLFPGVLTDRIADQ----VAGADVVAEPLgpHPEL 221


                 ....*....
gi 896153278 236 APIVCCRWD 244
Cdd:COG2138  222 ADLVLDRYR 230
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 3-107 1.43e-20

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: 83.39  E-value: 1.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   3 ALILLAHGSRHSETKPVLEDVVALVREKMPLTRldapsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAFHS 82
Cdd:cd03416    1 ALLLVGHGSRDPRAAEALEALAERLRERLPGDE------VELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHV 74

                         90       100
                 ....*....|....*....|....*..
gi 896153278  83 RVDVPEQVRLCDR--HGVDITVAEGLG 107
Cdd:cd03416   75 KEDIPAALAAARArhPGVRIRYAPPLG 101
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 9-107 6.88e-12

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: 60.33  E-value: 6.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278    9 HGSRHSETKPVLEDVVALVREKMPLTRldapsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAFHSRVDVPE 88
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLP------VEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPE 74

                          90       100
                  ....*....|....*....|.
gi 896153278   89 QVRLCDRH--GVDITVAEGLG 107
Cdd:pfam01903  75 ELAAAKAAhpDIEIRYAPPLG 95
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
1-123 7.16e-07

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 47.18  E-value: 7.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   1 MTALILLAHGSRHSETKPVLEDVVALVREKMPltrlDAPsqIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAF 80
Cdd:PRK00923   1 MLGLLLVGHGSRLPYNKEVVTKIAEKIKEKHP----FYI--VEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896153278  81 HSRVDVPEQVRL--CDRH-------GVDITVAEGLGLGDGTKRAVVKRIIEA 123
Cdd:PRK00923  75 HTKRDIPRILGLdeGEKEeieedgkDVEIVYAEPLGADERIADIVLKRANEA 126
Chelatase_Class_II cd03409
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze ...
 3-81 1.38e-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: 45.83  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   3 ALILLAHGSRHSETKP-VLEDVVALVREKMPltrldaPSQIRLAWLDLDEPSLDTVCAELAAAGETQALAVPLLFTDAFH 81
Cdd:cd03409    1 GLLVVGHGSPYKDPYKkDIEAQAHNLAESLP------DFPYYVGFQSGLGPDTEEAIRELAEEGYQRVVIVPLAPVSGDE 74
CbiX_SirB_C cd03414
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 2-124 4.50e-06

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: 44.52  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   2 TALILLAHGSRHSETKPVLEDVVALVREKMPLTRLDApsqirlAWLDLDEPSLDTVCAELAAAGETQALAVP-LLFTDAF 80
Cdd:cd03414    1 TAVVLVGRGSSDPDANADVAKIARLLEEGTGFARVET------AFAAATRPSLPEALERLRALGARRVVVLPyLLFTGVL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 896153278  81 HSRVDvpEQVR-LCDRHGVDITVAEGLGLGDGTKRAVVKRIIEAA 124
Cdd:cd03414   75 MDRIE--EQVAeLAAEPGIEFVLAPPLGPHPELAEALLERVREAL 117
PRK02395 PRK02395
hypothetical protein; Provisional
 2-125 1.10e-04

hypothetical protein; Provisional


Pssm-ID: 235034 [Multi-domain]  Cd Length: 279  Bit Score: 42.38  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278   2 TALILLAHGSRHSE-TKPVLEDVVALVREKmpltrlDAPSQIRLAWLDlDEPSLDTVCAELAAageTQALAVPLLFTDAF 80
Cdd:PRK02395 136 TALAVVGHGTERNEnSAKAIYYHADRLRER------GRFAEVEALFLD-EEPEVDDWPDLFEA---DDVVVVPLFIADGF 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896153278  81 HSRVDVPEQVRLCD-----------RHGVDITVAEGLGLGDGTKRAVVKRIIEAAE 125
Cdd:PRK02395 206 HTQEDIPEDMGLTDdyrtgydvptaVDGHRIWYAGAVGTEPLMADVILERAADAGA 261
CbiX_SirB_C cd03414
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 136-219 1.23e-04

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: 40.67  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896153278 136 LVMGVGSSDEDANAAVHQFAANLGGMLP-GHVSAAFVvgpeKIKGADAVAAAQERAAKRGRGLVVVPLFTAPGLLWDRVI 214
Cdd:cd03414    4 VLVGRGSSDPDANADVAKIARLLEEGTGfARVETAFA----AATRPSLPEALERLRALGARRVVVLPYLLFTGVLMDRIE 79


                 ....*
gi 896153278 215 DAGAA 219
Cdd:cd03414   80 EQVAE 84
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 141-214 7.09e-03

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: 35.29  E-value: 7.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896153278  141 GSSDEDANAAVHQFAANLGGMLPG-HVSAAF--VVGPekikgaDAVAAAQERAAKRGRGLVVVPLFTAPGLLWDRVI 214
Cdd:pfam01903   2 GSRDPEANEDFEQLARRLRELGPFlPVEVAFleLAEP------SLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDI 72
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH