thioredoxin-like (2Fe-2S) ferredoxin domain-containing protein is a soluble low-potential electron carrier containing a single (2Fe-2S) cluster; also contains a CbiX/SirB N-terminal domain belonging to the class II chelatase family of ATP-independent monomeric or homodimeric enzymes that catalyze the insertion of metal into protoporphyrin rings
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
83-215
2.57e-42
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: 142.77 E-value: 2.57e-42
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
89-192
4.19e-41
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: 135.83 E-value: 4.19e-41
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
83-183
1.13e-37
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: 126.92 E-value: 1.13e-37
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
83-215
2.57e-42
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: 142.77 E-value: 2.57e-42
CbiX; The function of CbiX is uncertain, however it is found in cobalamin biosynthesis operons ...
89-192
4.19e-41
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: 135.83 E-value: 4.19e-41
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
83-183
1.13e-37
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: 126.92 E-value: 1.13e-37
Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), ...
82-200
1.60e-25
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: 96.13 E-value: 1.60e-25
Sirohydrochlorin ferrochelatase [Coenzyme transport and metabolism]; Sirohydrochlorin ...
77-197
1.40e-21
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: 88.84 E-value: 1.40e-21
Archaeal sirohydrochlorin cobalt chelatase (CbiX) single domain. Proteins in this subgroup ...
84-160
7.84e-09
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: 52.15 E-value: 7.84e-09
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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