CBIK_SALTY
ID CBIK_SALTY Reviewed; 264 AA.
AC Q05592;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sirohydrochlorin cobaltochelatase;
DE EC=4.99.1.3;
GN Name=cbiK; OrderedLocusNames=STM2025;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RC STRAIN=LT2;
RX PubMed=8501034; DOI=10.1128/jb.175.11.3303-3316.1993;
RA Roth J.R., Lawrence J.G., Rubenfield M., Kieffer-Higgins S., Church G.M.;
RT "Characterization of the cobalamin (vitamin B12) biosynthetic genes of
RT Salmonella typhimurium.";
RL J. Bacteriol. 175:3303-3316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=1451790; DOI=10.1016/0014-5793(92)80213-z;
RA Roessner C.A., Warren M.J., Santander P.J., Atshaves B.P., Ozaki S.,
RA Stolowich N.J., Iida K., Scott A.I.;
RT "Expression of 9 Salmonella typhimurium enzymes for cobinamide synthesis.
RT Identification of the 11-methyl and 20-methyl transferases of corrin
RT biosynthesis.";
RL FEBS Lett. 301:73-78(1992).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9150215; DOI=10.1128/jb.179.10.3202-3212.1997;
RA Raux E., Thermes C., Heathcote P., Rambach A., Warren M.J.;
RT "A role for Salmonella typhimurium cbiK in cobalamin (vitamin B12) and
RT siroheme biosynthesis.";
RL J. Bacteriol. 179:3202-3212(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF GLU-89;
RP HIS-145; GLU-175; HIS-207 AND ASP-211.
RC STRAIN=LT2;
RX PubMed=10451360; DOI=10.1021/bi9906773;
RA Schubert H.L., Raux E., Wilson K.S., Warren M.J.;
RT "Common chelatase design in the branched tetrapyrrole pathways of heme and
RT anaerobic cobalamin synthesis.";
RL Biochemistry 38:10660-10669(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH
RP COBALT-SIROHYDROCHLORIN, AND REACTION MECHANISM.
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 -!- 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 -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 1/10.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10451360,
CC ECO:0000269|PubMed:21173279}.
CC -!- SIMILARITY: Belongs to the CbiK family. {ECO:0000305}.
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DR EMBL; L12006; AAA27262.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20929.1; -; Genomic_DNA.
DR RefSeq; NP_460970.1; NC_003197.2.
DR RefSeq; WP_000709784.1; NC_003197.2.
DR PDB; 1QGO; X-ray; 2.40 A; A=1-264.
DR PDB; 2XWP; X-ray; 1.90 A; A=1-264.
DR PDBsum; 1QGO; -.
DR PDBsum; 2XWP; -.
DR AlphaFoldDB; Q05592; -.
DR SMR; Q05592; -.
DR STRING; 99287.STM2025; -.
DR PaxDb; Q05592; -.
DR EnsemblBacteria; AAL20929; AAL20929; STM2025.
DR GeneID; 1253546; -.
DR KEGG; stm:STM2025; -.
DR PATRIC; fig|99287.12.peg.2147; -.
DR HOGENOM; CLU_036584_1_1_6; -.
DR OMA; FMFVAGD; -.
DR PhylomeDB; Q05592; -.
DR BioCyc; MetaCyc:MON-13175; -.
DR BioCyc; SENT99287:STM2025-MON; -.
DR UniPathway; UPA00148; UER00223.
DR EvolutionaryTrace; Q05592; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046906; F:tetrapyrrole binding; IDA:UniProtKB.
DR GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR010388; Anaerobic_Co-chelatase.
DR Pfam; PF06180; CbiK; 1.
DR PIRSF; PIRSF033579; Anaer_Co_chel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Cobalt; Direct protein sequencing;
KW Lyase; Metal-binding; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..264
FT /note="Sirohydrochlorin cobaltochelatase"
FT /id="PRO_0000218656"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 10
FT /ligand="substrate"
FT BINDING 85..92
FT /ligand="substrate"
FT BINDING 145
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT BINDING 175
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305"
FT BINDING 202..203
FT /ligand="substrate"
FT BINDING 207
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000305"
FT BINDING 207
FT /ligand="substrate"
FT MUTAGEN 89
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:10451360"
FT MUTAGEN 145
FT /note="H->A: No cobalt affinity."
FT /evidence="ECO:0000269|PubMed:10451360"
FT MUTAGEN 175
FT /note="E->A: Slightly reduced cobalt affinity."
FT /evidence="ECO:0000269|PubMed:10451360"
FT MUTAGEN 207
FT /note="H->A: Very reduced cobalt affinity."
FT /evidence="ECO:0000269|PubMed:10451360"
FT MUTAGEN 211
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:10451360"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 15..32
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1QGO"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1QGO"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:2XWP"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2XWP"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:2XWP"
SQ SEQUENCE 264 AA; 29239 MW; 34667EDACF603ECE CRC64;
MKKALLVVSF GTSYHDTCEK NIVACERDLA ASCPDRDLFR AFTSGMIIRK LRQRDGIDID
TPLQALQKLA AQGYQDVAIQ SLHIINGDEY EKIVREVQLL RPLFTRLTLG VPLLSSHNDY
VQLMQALRQQ MPSLRQTEKV VFMGHGASHH AFAAYACLDH MMTAQRFPAR VGAVESYPEV
DILIDSLRDE GVTGVHLMPL MLVAGDHAIN DMASDDGDSW KMRFNAAGIP ATPWLSGLGE
NPAIRAMFVA HLHQALNMAV EEAA
