BTUR_SALTY
ID BTUR_SALTY Reviewed; 196 AA.
AC P31570;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Corrinoid adenosyltransferase CobA;
DE EC=2.5.1.17;
DE AltName: Full=Cob(II)alamin adenosyltransferase;
DE AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase;
DE AltName: Full=Cobinamide/cobalamin adenosyltransferase;
GN Name=btuR; Synonyms=cobA {ECO:0000303|PubMed:7916712};
GN OrderedLocusNames=STM1718;
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].
RC STRAIN=LT2;
RX PubMed=7916712; DOI=10.1016/0378-1119(93)90701-4;
RA Suh S.-J., Escalante-Semerena J.C.;
RT "Cloning, sequencing and overexpression of cobA which encodes ATP:corrinoid
RT adenosyltransferase in Salmonella typhimurium.";
RL Gene 129:93-97(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 1-21, AND CHARACTERIZATION.
RX PubMed=7860601; DOI=10.1128/jb.177.4.921-925.1995;
RA Suh S.-J., Escalante-Semerena J.C.;
RT "Purification and initial characterization of the ATP:corrinoid
RT adenosyltransferase encoded by the cobA gene of Salmonella typhimurium.";
RL J. Bacteriol. 177:921-925(1995).
RN [4]
RP CHARACTERIZATION.
RX PubMed=2403541; DOI=10.1128/jb.172.1.273-280.1990;
RA Escalante-Semerena J.C., Suh S.-J., Roth J.R.;
RT "cobA function is required for both de novo cobalamin biosynthesis and
RT assimilation of exogenous corrinoids in Salmonella typhimurium.";
RL J. Bacteriol. 172:273-280(1990).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=11160088; DOI=10.1128/jb.183.5.1577-1584.2001;
RA Johnson C.L., Pechonick E., Park S.D., Havemann G.D., Leal N.A.,
RA Bobik T.A.;
RT "Functional genomic, biochemical, and genetic characterization of the
RT Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene.";
RL J. Bacteriol. 183:1577-1584(2001).
RN [6]
RP CHARACTERIZATION.
RX PubMed=12080060; DOI=10.1074/jbc.m203893200;
RA Fonseca M.V., Buan N.R., Horswill A.R., Rayment I.,
RA Escalante-Semerena J.C.;
RT "The ATP:Co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella
RT enterica requires the 2'-OH group of ATP for function and yields inorganic
RT triphosphate as its reaction byproduct.";
RL J. Biol. Chem. 277:33127-33131(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-183.
RX PubMed=11148030; DOI=10.1021/bi002145o;
RA Bauer C.B., Fonseca M.V., Holden H.M., Thoden J.B., Thompson T.B.,
RA Escalante-Semerena J.C., Rayment I.;
RT "Three-dimensional structure of ATP:corrinoid adenosyltransferase from
RT Salmonella typhimurium in its free state, complexed with MgATP, or
RT complexed with hydroxycobalamin and MgATP.";
RL Biochemistry 40:361-374(2001).
CC -!- FUNCTION: Required for both de novo synthesis of the corrin ring for
CC the assimilation of exogenous corrinoids. Participates in the
CC adenosylation of a variety of incomplete and complete corrinoids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-
CC transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3
CC H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate;
CC Xref=Rhea:RHEA:11528, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58503,
CC ChEBI:CHEBI:58537; EC=2.5.1.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + 2 cob(II)alamin + reduced [electron-transfer
CC flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized
CC [electron-transfer flavoprotein] + 2 triphosphate;
CC Xref=Rhea:RHEA:28671, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16304, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:18408, ChEBI:CHEBI:30616, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307; EC=2.5.1.17;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Mild growth defect on 1,2-propanediol-
CC cyanocobalamin medium; no growth is seen in a double cobA-pduO
CC deletion. {ECO:0000269|PubMed:11160088}.
CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L08890; AAA71929.1; -; Unassigned_DNA.
DR EMBL; AE006468; AAL20636.1; -; Genomic_DNA.
DR PIR; JN0721; JN0721.
DR RefSeq; NP_460677.1; NC_003197.2.
DR RefSeq; WP_001278856.1; NC_003197.2.
DR PDB; 1G5R; X-ray; 2.10 A; A=1-196.
DR PDB; 1G5T; X-ray; 1.80 A; A=1-196.
DR PDB; 1G64; X-ray; 2.10 A; A/B=1-196.
DR PDB; 4HUT; X-ray; 1.95 A; A/B=6-196.
DR PDBsum; 1G5R; -.
DR PDBsum; 1G5T; -.
DR PDBsum; 1G64; -.
DR PDBsum; 4HUT; -.
DR AlphaFoldDB; P31570; -.
DR SMR; P31570; -.
DR STRING; 99287.STM1718; -.
DR PaxDb; P31570; -.
DR EnsemblBacteria; AAL20636; AAL20636; STM1718.
DR GeneID; 1253237; -.
DR KEGG; stm:STM1718; -.
DR PATRIC; fig|99287.12.peg.1815; -.
DR HOGENOM; CLU_088595_0_0_6; -.
DR OMA; HAMGEGF; -.
DR PhylomeDB; P31570; -.
DR BioCyc; MetaCyc:MON-13220; -.
DR BioCyc; SENT99287:STM1718-MON; -.
DR BRENDA; 2.5.1.17; 2169.
DR UniPathway; UPA00148; UER00233.
DR EvolutionaryTrace; P31570; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00561; CobA_CobO_BtuR; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003724; CblAdoTrfase_CobA.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02572; CobA_CobO_BtuR; 1.
DR PIRSF; PIRSF015617; Adensltrnsf_CobA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00708; cobA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cobalamin biosynthesis; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Porphyrin biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..196
FT /note="Corrinoid adenosyltransferase CobA"
FT /id="PRO_0000065010"
FT BINDING 36..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:4HUT"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:1G5T"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1G5T"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:1G5T"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:1G5T"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:1G5T"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1G5T"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4HUT"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4HUT"
SQ SEQUENCE 196 AA; 21726 MW; AE02E11176513CC4 CRC64;
MSDERYQQRQ QKVKDRVDAR VAQAQEERGI IIVFTGNGKG KTTAAFGTAA RAVGHGKNVG
VVQFIKGTWP NGERNLLEPH GVEFQVMATG FTWETQNREA DTAACMAVWQ HGKRMLADPL
LDMVVLDELT YMVAYDYLPL EEVISALNAR PGHQTVIITG RGCHRDILDL ADTVSELRPV
KHAFDAGVKA QMGIDY
