CBIKC_DESVH
ID CBIKC_DESVH Reviewed; 282 AA.
AC Q72CB8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Sirohydrochlorin cobaltochelatase CbiKC;
DE EC=4.99.1.3;
DE AltName: Full=Sirohydrochlorin ferrochelatase CbiKC;
DE EC=4.99.1.4;
GN Name=cbiKc; OrderedLocusNames=DVU_1365;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=18457416; DOI=10.1021/bi800342c;
RA Lobo S.A., Brindley A.A., Romao C.V., Leech H.K., Warren M.J.,
RA Saraiva L.M.;
RT "Two distinct roles for two functional cobaltochelatases (CbiK) in
RT Desulfovibrio vulgaris hildenborough.";
RL Biochemistry 47:5851-5857(2008).
CC -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as
CC part of the anaerobic pathway to cobalamin biosynthesis. To a lesser
CC extent, is also able to insert Fe(2+) into sirohydrochlorin, yielding
CC siroheme. {ECO:0000269|PubMed:18457416}.
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:0000269|PubMed:18457416};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC Evidence={ECO:0000269|PubMed:18457416};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 1/10.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18457416}.
CC -!- MISCELLANEOUS: Desulfovibrio vulgaris possesses two versions of CbiK
CC encoded within the genome, one cytoplasmic (CbiKC) and one periplasmic
CC (CbiKP).
CC -!- SIMILARITY: Belongs to the CbiK family. {ECO:0000305}.
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DR EMBL; AE017285; AAS95843.1; -; Genomic_DNA.
DR RefSeq; WP_010938660.1; NC_002937.3.
DR RefSeq; YP_010584.1; NC_002937.3.
DR AlphaFoldDB; Q72CB8; -.
DR SMR; Q72CB8; -.
DR STRING; 882.DVU_1365; -.
DR PaxDb; Q72CB8; -.
DR EnsemblBacteria; AAS95843; AAS95843; DVU_1365.
DR KEGG; dvu:DVU_1365; -.
DR PATRIC; fig|882.5.peg.1276; -.
DR eggNOG; COG4822; Bacteria.
DR HOGENOM; CLU_036584_1_1_7; -.
DR OMA; CIDPIEN; -.
DR PhylomeDB; Q72CB8; -.
DR BRENDA; 4.99.1.3; 1914.
DR UniPathway; UPA00148; UER00223.
DR UniPathway; UPA00262; UER00376.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IDA:UniProtKB.
DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IDA:UniProtKB.
DR GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; TAS:UniProtKB.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
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 Cobalamin biosynthesis; Cobalt; Cytoplasm; Lyase; Metal-binding;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..282
FT /note="Sirohydrochlorin cobaltochelatase CbiKC"
FT /id="PRO_0000407986"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102..110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250"
FT BINDING 223..224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 282 AA; 30825 MW; D967A5441F2DF69F CRC64;
MVPPRWGSLD SLKPQQHLPM TKKGILLAAF GSGNRQGEST LRLFDERVRE RFPGVPVRWA
FTSVIMRRRL AAARKKTDSV LKALQKMWFE KYTHVAVQSL HIIPGAEYGD LVADVEAMRR
DDGFTAATVG APLLAGSGDM ERSAAALLAH LPAGRKPDEA VVFMGHGTRH PAESSYEALA
ALVRRVDPHV HIGTMGGSRT LDHILPELQQ GGVKGVWLMP LLSVVGRHAT EDMAGTDPES
WKSRLEASGL RCIPVLRGTA EYEGFVDIWL DHLTAAVSAL DD
