CBIKP_DESVH
ID CBIKP_DESVH Reviewed; 297 AA.
AC Q72EC8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Sirohydrochlorin cobaltochelatase CbiKP;
DE EC=4.99.1.3;
DE AltName: Full=Sirohydrochlorin ferrochelatase CbiKP;
DE EC=4.99.1.4;
DE Flags: Precursor;
GN Name=cbiKp; OrderedLocusNames=DVU_0650;
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 PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, HEME-BINDING,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-297 OF COMPLEXES WITH HEME AND
RP COBALT.
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. To a
CC lesser extent, is also able to insert Fe(2+) into sirohydrochlorin,
CC yielding siroheme. Its periplasmic location means that it cannot
CC participate in cobalamin biosynthesis and its genomic environment
CC suggests it is likely to be associated with a heme or metal transport
CC system. {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 -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:18457416}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:18457416}.
CC -!- MISCELLANEOUS: Binds 1 heme b (iron-protoporphyrin IX) group per dimer,
CC which is not required for chelatase activity but may be linked to the
CC putative transport function.
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; AAS95131.1; -; Genomic_DNA.
DR RefSeq; WP_010937953.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009872.1; NC_002937.3.
DR PDB; 2XVX; X-ray; 1.90 A; A=29-297.
DR PDB; 2XVY; X-ray; 1.70 A; A=29-297.
DR PDB; 2XVZ; X-ray; 2.40 A; A=29-297.
DR PDBsum; 2XVX; -.
DR PDBsum; 2XVY; -.
DR PDBsum; 2XVZ; -.
DR AlphaFoldDB; Q72EC8; -.
DR SMR; Q72EC8; -.
DR DIP; DIP-59587N; -.
DR STRING; 882.DVU_0650; -.
DR PaxDb; Q72EC8; -.
DR PRIDE; Q72EC8; -.
DR EnsemblBacteria; AAS95131; AAS95131; DVU_0650.
DR KEGG; dvu:DVU_0650; -.
DR PATRIC; fig|882.5.peg.607; -.
DR eggNOG; COG4822; Bacteria.
DR HOGENOM; CLU_036584_1_0_7; -.
DR OMA; FMFVAGD; -.
DR PhylomeDB; Q72EC8; -.
DR BRENDA; 4.99.1.3; 1914.
DR EvolutionaryTrace; Q72EC8; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0042597; C:periplasmic space; TAS:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
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; IEA:InterPro.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR InterPro; IPR010388; Anaerobic_Co-chelatase.
DR Pfam; PF06180; CbiK; 1.
DR PIRSF; PIRSF033579; Anaer_Co_chel; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Direct protein sequencing; Heme; Iron; Lyase;
KW Metal-binding; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:18457416"
FT CHAIN 29..297
FT /note="Sirohydrochlorin cobaltochelatase CbiKP"
FT /id="PRO_0000407985"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117..125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared between dimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 182
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT BINDING 212
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT BINDING 239..240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2XVY"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:2XVY"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:2XVY"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2XVY"
FT HELIX 279..294
FT /evidence="ECO:0007829|PDB:2XVY"
SQ SEQUENCE 297 AA; 31807 MW; EB6947A9C176295A CRC64;
MSRHPMVTRL LCLVFSCLII LACSPAFAGH GAPKAQKTGI LLVAFGTSVE EARPALDKMG
DRVRAAHPDI PVRWAYTAKM IRAKLRAEGI AAPSPAEALA GMAEEGFTHV AVQSLHTIPG
EEFHGLLETA HAFQGLPKGL TRVSVGLPLI GTTADAEAVA EALVASLPAD RKPGEPVVFM
GHGTPHPADI CYPGLQYYLW RLDPDLLVGT VEGSPSFDNV MAELDVRKAK RVWLMPLMAV
AGDHARNDMA GDEDDSWTSQ LARRGIEAKP VLHGTAESDA VAAIWLRHLD DALARLN
