ID A0A1A9EVD8_9GAMM Unreviewed; 594 AA.
AC A0A1A9EVD8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Oxaloacetate decarboxylase subunit alpha {ECO:0000313|EMBL:ANG61628.1};
GN ORFNames=A8C75_03495 {ECO:0000313|EMBL:ANG61628.1};
OS Marinobacterium aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG61628.1, ECO:0000313|Proteomes:UP000078070};
RN [1] {ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA Baek K., Yang S.-J.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANG61628.1, ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|EMBL:ANG61628.1,
RC ECO:0000313|Proteomes:UP000078070};
RX PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA Bae S.S., Jung J., Chung D., Baek K.;
RT "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT isolated from estuary sediment.";
RL Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP015839; ANG61628.1; -; Genomic_DNA.
DR RefSeq; WP_067378169.1; NZ_CP015839.1.
DR AlphaFoldDB; A0A1A9EVD8; -.
DR STRING; 1821621.A8C75_03495; -.
DR KEGG; mars:A8C75_03495; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000078070; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000078070}.
FT DOMAIN 8..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 523..594
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 594 AA; 64438 MW; 8CBCB088EBCF3D92 CRC64;
MSDAKKPLGI TELVLRDGHQ SLLATRMRLD DMLPIADKLD QVGYWSTESW GGATFDSCIR
YIGEDPWDRI RELKKAMPNT RQQMLLRGQN LLGYRHYADD VVARFVERAA TNGVDVFRIF
DAMNDPRNLA AAIKAVKATG KHAQGTLSYT TSSVHTLDNW VDYAKTLEDM GAESICIKDM
SGILKPYEAF DLVSRLKNQT QLEVQLQSHA TSGLADMTLL KAIEAGIDRV DTSISSMSMT
YGHTATETVV ATLDGTDRDT GLNLELLEEI AAYFRDVRKK YAKFEGSLRG TDSRILIAQV
PGGMLTNMES QLREQGAADK FDEVLAEIPR VRADLGLIPL VTPTSQIVGT QAVINVLMGE
RYKSISKEVQ AILKGEYGAA PAPYNAELQA RVLDGKDPIT CRPADMLEPE IERLTVELRK
QAQEKGISLA TGDNEIDDVL TYALFPQIGL KFLENRANPD AFEPVPTLED AQTMAAPKKS
GPEVYTITVN GQNYVVQVAE GGDISAISKA PVAAAAPAAP TVAEGEDVPA PLAGNIWKVE
VGVGQAVQEG DVLVILEAMK METEVRAARA GTVVAVDVKE GDAVQVGDAL LSLA
//