ID A0A0D8CS49_9GAMM Unreviewed; 597 AA.
AC A0A0D8CS49;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Oxaloacetate decarboxylase {ECO:0000313|EMBL:KJE39085.1};
GN ORFNames=SG35_22180 {ECO:0000313|EMBL:KJE39085.1};
OS Thalassomonas actiniarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassomonas.
OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE39085.1};
RN [1] {ECO:0000313|EMBL:KJE39085.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE39085.1};
RA Olonade I., van Zyl L.J., Tuffin M.I.;
RT "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT actiniarum.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KJE39085.1}.
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DR EMBL; JYNI01000052; KJE39085.1; -; Genomic_DNA.
DR RefSeq; WP_044834675.1; NZ_CP059735.1.
DR AlphaFoldDB; A0A0D8CS49; -.
DR STRING; 485447.SG35_22180; -.
DR PATRIC; fig|485447.4.peg.4883; -.
DR OrthoDB; 9760256at2; -.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005776; OadA.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01108; oadA; 1.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267}.
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 522..597
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 597 AA; 64545 MW; B6B1A36B08D79B5D CRC64;
MTKPLGITEV VLRDGHQSLL ATRLRLEDML PIASKLDDIG YWSIESWGGA TFDSCIRYLG
EDPWERIRAL KKAMPKTKQQ MLFRGQNILG YRHYADDVVE KFVERAHVNG IDVFRIFDAM
NDVRNLQTAV KAAVKVGAHA QGTLSYTESP VHTLEGWLTM AKQLEDMGAH SLCIKDMAGL
LKPYDGAELI SRLKETVSLP IALHCHATTG LSIATHMKAI DADIDVIDTS ISSMSMTYGH
SPTETLVSIV EGTERDTGLD MVKLAEVAAY FREVREKYAQ FEGSLKGVDA RILLAQVPGG
MLTNMESQLK EQGAADRLDE VLTEIPKVRK DLGYIPLVTP TSQIVGTQAV LNVLTGERYK
SITKETSGVL KGEYGATADK VNAELQARVL NGEQAITCRP ADLLSPEMDK LTVELEQLAQ
EKGISLAPEA VDDVLTYALF PQIGLKFLEN RDNADAFEPK PSTITAQDKE AAQAAPTAPA
TAAAESYAVS VDGKVYDVVV GPGGAIKDIS YAAVGDEAIK QSASVSAEET LNAPLAGNIF
KVLVKPGDRV AANDVVIIME AMKMETEVRA VTDGEITTLH AKEGDSVAVG EALLSLV
//