CBIX_ARCFU
ID CBIX_ARCFU Reviewed; 132 AA.
AC O29537;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sirohydrochlorin cobaltochelatase {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000303|PubMed:16835730};
DE EC=4.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000269|PubMed:16835730};
DE AltName: Full=CbiXS {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000303|PubMed:16835730};
GN Name=cbiX {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000303|PubMed:16835730};
GN Synonyms=cbiXS {ECO:0000303|PubMed:16835730};
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND SUBUNIT.
RX PubMed=16835730; DOI=10.1007/s10969-006-9008-x;
RA Yin J., Xu L.X., Cherney M.M., Raux-Deery E., Bindley A.A., Savchenko A.,
RA Walker J.R., Cuff M.E., Warren M.J., James M.N.;
RT "Crystal structure of the vitamin B12 biosynthetic cobaltochelatase, CbiXS,
RT from Archaeoglobus fulgidus.";
RL J. Struct. Funct. Genomics 7:37-50(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP COBALT-SIROHYDROCHLORIN, ACTIVE SITE, AND SUBUNIT.
RX PubMed=21173279; DOI=10.1073/pnas.1014298108;
RA Romao C.V., Ladakis D., Lobo S.A., Carrondo M.A., Brindley A.A., Deery E.,
RA Matias P.M., Pickersgill R.W., Saraiva L.M., Warren M.J.;
RT "Evolution in a family of chelatases facilitated by the introduction of
RT active site asymmetry and protein oligomerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:97-102(2011).
CC -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as
CC part of the anaerobic pathway to cobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000269|PubMed:16835730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin;
CC Xref=Rhea:RHEA:15893, ChEBI:CHEBI:15378, ChEBI:CHEBI:48828,
CC ChEBI:CHEBI:58351, ChEBI:CHEBI:60049; EC=4.99.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00785,
CC ECO:0000269|PubMed:16835730};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 1/10. {ECO:0000255|HAMAP-Rule:MF_00785,
CC ECO:0000305|PubMed:16835730}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00785, ECO:0000269|PubMed:16835730,
CC ECO:0000269|PubMed:21173279}.
CC -!- SIMILARITY: Belongs to the CbiX family. CbiXS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00785, ECO:0000305}.
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DR EMBL; AE000782; AAB90530.1; -; Genomic_DNA.
DR PIR; A69340; A69340.
DR RefSeq; WP_010878224.1; NC_000917.1.
DR PDB; 1TJN; X-ray; 2.01 A; A=1-132.
DR PDB; 2DJ5; X-ray; 2.55 A; A/B=1-132.
DR PDB; 2XWQ; X-ray; 2.01 A; A/B/C/D=1-132.
DR PDB; 2XWS; X-ray; 1.60 A; A=1-132.
DR PDBsum; 1TJN; -.
DR PDBsum; 2DJ5; -.
DR PDBsum; 2XWQ; -.
DR PDBsum; 2XWS; -.
DR AlphaFoldDB; O29537; -.
DR SMR; O29537; -.
DR DIP; DIP-59586N; -.
DR STRING; 224325.AF_0721; -.
DR EnsemblBacteria; AAB90530; AAB90530; AF_0721.
DR GeneID; 24794319; -.
DR KEGG; afu:AF_0721; -.
DR eggNOG; arCOG02246; Archaea.
DR HOGENOM; CLU_065901_2_1_2; -.
DR OMA; VICDPIG; -.
DR OrthoDB; 93992at2157; -.
DR PhylomeDB; O29537; -.
DR BRENDA; 4.99.1.3; 414.
DR UniPathway; UPA00148; UER00223.
DR EvolutionaryTrace; O29537; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IDA:UniProtKB.
DR GO; GO:0046906; F:tetrapyrrole binding; IDA:UniProtKB.
DR GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; TAS:UniProtKB.
DR HAMAP; MF_00785; CbiX; 1.
DR InterPro; IPR002762; CbiX-like.
DR InterPro; IPR023652; SiroHydchlorin_Cochelatase.
DR Pfam; PF01903; CbiX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Cobalt; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..132
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000150353"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785,
FT ECO:0000305|PubMed:21173279"
FT BINDING 10
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785,
FT ECO:0000305|PubMed:16835730, ECO:0000305|PubMed:21173279"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785,
FT ECO:0000269|PubMed:21173279, ECO:0007744|PDB:2XWQ"
FT BINDING 69..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785,
FT ECO:0000269|PubMed:21173279, ECO:0007744|PDB:2XWQ"
FT BINDING 74
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785,
FT ECO:0000305|PubMed:16835730, ECO:0000305|PubMed:21173279"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2XWS"
FT HELIX 15..31
FT /evidence="ECO:0007829|PDB:2XWS"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:2XWS"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:2XWS"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2XWS"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2XWQ"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2XWS"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2XWS"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2XWS"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2XWS"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2XWS"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:2XWS"
SQ SEQUENCE 132 AA; 15109 MW; 61B97A773EC78BB7 CRC64;
MRRGLVIVGH GSQLNHYREV MELHRKRIEE SGAFDEVKIA FAARKRRPMP DEAIREMNCD
IIYVVPLFIS YGLHVTEDLP DLLGFPRGRG IKEGEFEGKK VVICEPIGED YFVTYAILNS
VFRIGRDGKG EE
