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Conserved domains on  [gi|2788633833|ref|WP_370593294|]
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sirohydrochlorin chelatase [Rugamonas sp. CCM 8940]

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 ...
 5-130 4.90e-35

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: 120.42  E-value: 4.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   5 MPQRGLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLR 84
Cdd:COG2138     1 MMKTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2788633833  85 DLPLLLEQLRQEHPGVAFQVAGAVGEDPTVLAAMTDYCVNAAGDAA 130
Cdd:COG2138    81 DIPEALAEARARYPGVRIRLAPPLGPDPRLADLLAERLAEALARPD 126
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 5-130 4.90e-35

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: 120.42  E-value: 4.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   5 MPQRGLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLR 84
Cdd:COG2138     1 MMKTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2788633833  85 DLPLLLEQLRQEHPGVAFQVAGAVGEDPTVLAAMTDYCVNAAGDAA 130
Cdd:COG2138    81 DIPEALAEARARYPGVRIRLAPPLGPDPRLADLLAERLAEALARPD 126
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 9-109 1.92e-29

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: 102.26  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLPL 88
Cdd:cd03416     1 ALLLVGHGSRDPRAAEALEALAERLRERLPGDEVELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHVKEDIPA 80

                          90       100
                  ....*....|....*....|.
gi 2788633833  89 LLEQLRQEHPGVAFQVAGAVG 109
Cdd:cd03416    81 ALAAARARHPGVRIRYAPPLG 101
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 15-118 2.35e-26

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: 94.61  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833  15 HGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLPLLLEQLR 94
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLPVEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPEELAAAK 80

                          90       100
                  ....*....|....*....|....
gi 2788633833  95 QEHPGVAFQVAGAVGEDPTVLAAM 118
Cdd:pfam01903  81 AAHPDIEIRYAPPLGPHPLLAELL 104
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
9-90 1.44e-13

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 62.59  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLPL 88
Cdd:PRK00923    3 GLLLVGHGSRLPYNKEVVTKIAEKIKEKHPFYIVEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGVHTKRDIPR 82


                  ..
gi 2788633833  89 LL 90
Cdd:PRK00923   83 IL 84
 
Name Accession Description Interval E-value
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 5-130 4.90e-35

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: 120.42  E-value: 4.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   5 MPQRGLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLR 84
Cdd:COG2138     1 MMKTALLLVAHGSRDPEGAEEFEALAARLRARLPGLPVELAFLELAEPSLEEALDALVAQGATRIVVVPLFLAAGGHVKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2788633833  85 DLPLLLEQLRQEHPGVAFQVAGAVGEDPTVLAAMTDYCVNAAGDAA 130
Cdd:COG2138    81 DIPEALAEARARYPGVRIRLAPPLGPDPRLADLLAERLAEALARPD 126
CbiX_SirB_N cd03416
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 9-109 1.92e-29

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: 102.26  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLPL 88
Cdd:cd03416     1 ALLLVGHGSRDPRAAEALEALAERLRERLPGDEVELAFLELAEPSLAEALDELAAQGATRIVVVPLFLLAGGHVKEDIPA 80

                          90       100
                  ....*....|....*....|.
gi 2788633833  89 LLEQLRQEHPGVAFQVAGAVG 109
Cdd:cd03416    81 ALAAARARHPGVRIRYAPPLG 101
CbiX pfam01903
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
 15-118 2.35e-26

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: 94.61  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833  15 HGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLPLLLEQLR 94
Cdd:pfam01903   1 HGSRDPEANEDFEQLARRLRELGPFLPVEVAFLELAEPSLEEALRELVAQGVRRIVVVPLFLFAGGHVKRDIPEELAAAK 80

                          90       100
                  ....*....|....*....|....
gi 2788633833  95 QEHPGVAFQVAGAVGEDPTVLAAM 118
Cdd:pfam01903  81 AAHPDIEIRYAPPLGPHPLLAELL 104
PRK00923 PRK00923
sirohydrochlorin nickelochelatase;
9-90 1.44e-13

sirohydrochlorin nickelochelatase;


Pssm-ID: 234865 [Multi-domain]  Cd Length: 126  Bit Score: 62.59  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLPL 88
Cdd:PRK00923    3 GLLLVGHGSRLPYNKEVVTKIAEKIKEKHPFYIVEVGFMEFNEPTIPEALKKLIGTGADKIIVVPVFLAHGVHTKRDIPR 82


                  ..
gi 2788633833  89 LL 90
Cdd:PRK00923   83 IL 84
Chelatase_Class_II cd03409
Class II Chelatase: a family of ATP-independent monomeric or homodimeric enzymes that catalyze ...
 9-94 1.49e-09

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: 51.61  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGARAAS-WAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLP 87
Cdd:cd03409     1 GLLVVGHGSPYKDpYKKDIEAQAHNLAESLPDFPYYVGFQSGLGPDTEEAIRELAEEGYQRVVIVPLAPVSGDEVFYDID 80


                  ....*..
gi 2788633833  88 LLLEQLR 94
Cdd:cd03409    81 SEIGLVR 87
PLN02757 PLN02757
sirohydrochlorine ferrochelatase
 9-129 1.76e-09

sirohydrochlorine ferrochelatase


Pssm-ID: 215403 [Multi-domain]  Cd Length: 154  Bit Score: 52.44  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDLPL 88
Cdd:PLN02757   15 GVVIVDHGSRRKESNLMLEEFVAMYKQKTGHPIVEPAHMELAEPSIKDAFGRCVEQGASRVIVSPFFLSPGRHWQEDIPA 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2788633833  89 LLEQLRQEHPGVAFQVAGAVGEDPTVLAAMTD---YCV-NAAGDA 129
Cdd:PLN02757   95 LTAEAAKEHPGVKYLVTAPIGLHELMVDVVNDrikYCLsHVAGDA 139
CbiX_SirB_C cd03414
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
 9-120 8.33e-08

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: 47.21  E-value: 8.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGARAASWAAPFERLRDMTQARMPDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGghvlrdlpL 88
Cdd:cd03414     2 AVVLVGRGSSDPDANADVAKIARLLEEGTGFARVETAFAAATRPSLPEALERLRALGARRVVVLPYLLFTG--------V 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2788633833  89 LLEQLR------QEHPGVAFQVAGAVGEDPTVLAAMTD 120
Cdd:cd03414    74 LMDRIEeqvaelAAEPGIEFVLAPPLGPHPELAEALLE 111
SirB COG2138
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
 2-118 4.09e-05

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: 41.07  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   2 APTMPQRGLILFAHGARAASWAAPFERLRDMTQARMPdaRVALAFLElMTPQLPELAAQLVADGVAQITVVPVFLGQGGH 81
Cdd:COG2138   121 ALARPDTAVVLVGRGSSDPDANADVAKLARLLAERLG--PVETAFLG-TGPSLEEALERLRALGARRVVVLPYFLFPGVL 197

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2788633833  82 VLRDLPLLLEQLRqehpgvafqVAGAVGEDPTVLAAM 118
Cdd:COG2138   198 TDRIADQVAGADV---------VAEPLGPHPELADLV 225
PRK05782 PRK05782
bifunctional sirohydrochlorin cobalt chelatase/precorrin-8X methylmutase; Validated
 10-86 6.14e-04

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


Pssm-ID: 235605 [Multi-domain]  Cd Length: 335  Bit Score: 38.25  E-value: 6.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788633833  10 LILFAHGARAASWAAPFERLRDMTQARMpDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDL 86
Cdd:PRK05782    9 IILIGHGSRRETFNSDMEGMANYLKEKL-GVPIYLTYNEFAEPNWRSLLNEIIKEGYRRVIIALAFLGRGNHVFRDI 84
PRK02395 PRK02395
hypothetical protein; Provisional
 9-130 1.51e-03

hypothetical protein; Provisional


Pssm-ID: 235034 [Multi-domain]  Cd Length: 279  Bit Score: 36.99  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2788633833   9 GLILFAHGAR--AASWAAPF---ERLRDMTQArmpdARVALAFLElMTPQLPELAAQLVADgvaQITVVPVFLGQGGHVL 83
Cdd:PRK02395  137 ALAVVGHGTErnENSAKAIYyhaDRLRERGRF----AEVEALFLD-EEPEVDDWPDLFEAD---DVVVVPLFIADGFHTQ 208

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2788633833  84 RDLPLLL---------EQLRQEHPGVAFQVAGAVGEDPtvlaAMTDYCVNAAGDAA 130
Cdd:PRK02395  209 EDIPEDMgltddyrtgYDVPTAVDGHRIWYAGAVGTEP----LMADVILERAADAG 260
CbiX_CbiC cd03415
Archaeal sirohydrochlorin cobalt chelatase (CbiX) single domain. Proteins in this subgroup ...
 10-86 2.36e-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: 35.58  E-value: 2.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2788633833  10 LILFAHGARAASWAAPFERLRDMTQARMpDARVALAFLELMTPQLPELAAQLVADGVAQITVVPVFLGQGGHVLRDL 86
Cdd:cd03415     3 IIIITHGSRRNTFNEDMEEWAAYLERKL-GVPVYLTYNEYAEPNWRDLLNELLSEGYGHIIIALAFLGRGNHVARDI 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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