ID A8T042_9VIBR Unreviewed; 534 AA.
AC A8T042;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative propionyl-CoA carboxylase (Beta subunit) protein {ECO:0000313|EMBL:EDP60628.1};
GN ORFNames=AND4_06909 {ECO:0000313|EMBL:EDP60628.1};
OS Vibrio sp. AND4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP60628.1, ECO:0000313|Proteomes:UP000005159};
RN [1] {ECO:0000313|EMBL:EDP60628.1, ECO:0000313|Proteomes:UP000005159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AND4 {ECO:0000313|EMBL:EDP60628.1,
RC ECO:0000313|Proteomes:UP000005159};
RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA Milton D.L., Gonzalez J.M., Pinhassi J.;
RT "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT starvation.";
RL PLoS Biol. 8:E1000358-E1000358(2010).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP60628.1}.
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DR EMBL; ABGR01000001; EDP60628.1; -; Genomic_DNA.
DR RefSeq; WP_009841086.1; NZ_ABGR01000001.1.
DR AlphaFoldDB; A8T042; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000005159; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 4: Predicted;
FT DOMAIN 22..278
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 280..526
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 534 AA; 58363 MW; FF859E3BD4F1F93D CRC64;
MAIIKSKAKP TGELFLSNKT AMTELVQNLT ANIQAIKQGG GQKAIDRQRQ KGKLPVRERV
QHLLDEGSEF LEVGLFAAWN VYEESIPCAG VVAGIGTIEG IQCMVIANDP SVKGGTYYPL
TVKKHLRAQE IAQRCQLPCV YLVDSGGANL PHQADVFPDK EHFGRIFFNQ ARMSAQGIPQ
VAVVMGLCTA GGAYVPAMAD VSIMVKEQGT IFLAGPPLVK AATGEIVTDE ELGGADVHCR
KSGVADYYAQ NDQHALQLAR EAISNTNQPT PIQSDNPILP PRYDAEEMYG IVNANLRLSF
DVREIIARIV DDSDFDEFKA LYGKTLVCGF ARIQGSLIGI VANNGILFSE SSQKGAHFIE
LCAKRKLPLL FLQNITGFMV GKKFEAEGIA KHGAKLVMAV ACADVPKFTV IIGGSYGAGN
YGMCGRSYDP TMMWMWPNAR ISVMGGEQAA GVLTQVRREV KKRRSEDWPE KEESAFRDSI
IDLYESQGHP YYASARLWDD GIIDPKETRH VLTLALKAAR TAPIPDSNFG IFRM
//