ID   SGCOT_AGRFC             Reviewed;         400 AA.
AC   Q7CXU0;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Succinate--glutarate CoA-transferase {ECO:0000305};
DE            EC=2.8.3.- {ECO:0000269|PubMed:33154364};
GN   Name=caiB {ECO:0000303|PubMed:33154364};
GN   OrderedLocusNames=Atu2127 {ECO:0000312|EMBL:AAK87874.2};
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=33154364; DOI=10.1038/s41467-020-19251-5;
RA   Hu Y., Cronan J.E.;
RT   "Alpha-proteobacteria synthesize biotin precursor pimeloyl-ACP using BioZ
RT   3-ketoacyl-ACP synthase and lysine catabolism.";
RL   Nat. Commun. 11:5598-5598(2020).
CC   -!- FUNCTION: Is involved in L-lysine degradation and provides glutaryl-CoA
CC       for biotin synthesis. Catalyzes the conversion of glutarate to
CC       glutaryl-CoA via the transfer of CoA from succinyl-CoA.
CC       {ECO:0000269|PubMed:33154364}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutarate + succinyl-CoA = glutaryl-CoA + succinate;
CC         Xref=Rhea:RHEA:67900, ChEBI:CHEBI:30031, ChEBI:CHEBI:30921,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57378;
CC         Evidence={ECO:0000269|PubMed:11743194};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67901;
CC         Evidence={ECO:0000269|PubMed:11743194};
CC   -!- PATHWAY: Amino-acid degradation. {ECO:0000269|PubMed:33154364}.
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000269|PubMed:33154364}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to biotin
CC       auxotrophy. {ECO:0000269|PubMed:33154364}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; AE007869; AAK87874.2; -; Genomic_DNA.
DR   RefSeq; NP_355089.2; NC_003062.2.
DR   RefSeq; WP_010972076.1; NC_003062.2.
DR   SMR; Q7CXU0; -.
DR   STRING; 176299.Atu2127; -.
DR   EnsemblBacteria; AAK87874; AAK87874; Atu2127.
DR   KEGG; atu:Atu2127; -.
DR   PATRIC; fig|176299.10.peg.2140; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_033975_0_0_5; -.
DR   OMA; IIAGPYC; -.
DR   PhylomeDB; Q7CXU0; -.
DR   BioCyc; MetaCyc:MON-21427; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000000813; Chromosome circular.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   1: Evidence at protein level;
KW   Biotin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..400
FT                   /note="Succinate--glutarate CoA-transferase"
FT                   /id="PRO_0000453796"
FT   ACT_SITE        181
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P69902"
SQ   SEQUENCE   400 AA;  43385 MW;  0127F21CFA67C43E CRC64;
     MTDMPNRKPP LSGIRVIELA RVLAGPWAGQ MLADMGADVI KVENPEGGDD TRAWGPPFVE
     SADGENLSAA YYHATNRGKR SIVADLKTPE GCALVRRLVR TADVVIENFK RDGLAKYGLD
     YESLRVLNPK LIYCSITGFG QTGPYADFAG YDYIVQGMSG FMSITGEPDG QPMKAGVAVA
     DIFTGIYSVS AIQAALIHAM RSGEGQHIDM ALLDVQSAVL ANQNMNYLIS GRPPIRLGNA
     HPNISPYEVV PTADGFLILA VGNDGQFRRL CNILGIGAIA DDERYATNKA RVAHKVEVRQ
     IISTETLKWN KRDLLTACET NAVPAGPINS IEEMFADPQV QARGLRVDLE AEDGTVIPGV
     RTPIIMSQTP LRYERPSPKL GEHQAQVLAE LETIERTATP