CBIX_SULAC
ID CBIX_SULAC Reviewed; 123 AA.
AC Q4JAI2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Sirohydrochlorin cobaltochelatase {ECO:0000255|HAMAP-Rule:MF_00785};
DE EC=4.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00785};
DE AltName: Full=CbiXS {ECO:0000255|HAMAP-Rule:MF_00785};
GN Name=cbiX {ECO:0000255|HAMAP-Rule:MF_00785}; OrderedLocusNames=Saci_0830;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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}.
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 -!- 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 -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00785}.
CC -!- SIMILARITY: Belongs to the CbiX family. CbiXS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00785}.
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DR EMBL; CP000077; AAY80197.1; -; Genomic_DNA.
DR RefSeq; WP_011277699.1; NC_007181.1.
DR AlphaFoldDB; Q4JAI2; -.
DR SMR; Q4JAI2; -.
DR STRING; 330779.Saci_0830; -.
DR EnsemblBacteria; AAY80197; AAY80197; Saci_0830.
DR GeneID; 3472666; -.
DR KEGG; sai:Saci_0830; -.
DR PATRIC; fig|330779.12.peg.794; -.
DR eggNOG; arCOG02246; Archaea.
DR HOGENOM; CLU_065901_2_1_2; -.
DR OMA; HEHEKLE; -.
DR UniPathway; UPA00148; UER00223.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00785; CbiX; 1.
DR InterPro; IPR002762; CbiX-like.
DR InterPro; IPR023652; SiroHydchlorin_Cochelatase.
DR Pfam; PF01903; CbiX; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Cobalt; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..123
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000150361"
FT ACT_SITE 9
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 9
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 68..73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
FT BINDING 73
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00785"
SQ SEQUENCE 123 AA; 13941 MW; 79E4FB988B526709 CRC64;
MIGLLLVLHG SKIKEWQEIV INYAEELKRH FPLVEYGFIE INEPKIDEAA KKLVERGADT
IVVVPLLFAA GMHFKRDIPN QLKETSNKAK IIIAEPIGFD KRIVDILKEK AEKALSVEGT
SYQ
