ID U1K456_9GAMM Unreviewed; 593 AA.
AC U1K456;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Oxaloacetate decarboxylase {ECO:0000313|EMBL:ERG27282.1};
DE EC=4.1.1.3 {ECO:0000313|EMBL:ERG27282.1};
GN ORFNames=PMAN_04102 {ECO:0000313|EMBL:ERG27282.1};
OS Pseudoalteromonas marina DSM 17587.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117316 {ECO:0000313|EMBL:ERG27282.1, ECO:0000313|Proteomes:UP000016528};
RN [1] {ECO:0000313|EMBL:ERG27282.1, ECO:0000313|Proteomes:UP000016528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17587 {ECO:0000313|Proteomes:UP000016528};
RX PubMed=22535931; DOI=10.1128/JB.00265-12;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA He H.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of type strains of seven species of the marine bacterium
RT Pseudoalteromonas.";
RL J. Bacteriol. 194:2746-2747(2012).
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:ERG27282.1}.
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DR EMBL; AHCB02000005; ERG27282.1; -; Genomic_DNA.
DR AlphaFoldDB; U1K456; -.
DR Proteomes; UP000016528; Unassembled WGS sequence.
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 Lyase {ECO:0000313|EMBL:ERG27282.1}.
FT DOMAIN 4..264
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 518..593
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 593 AA; 64663 MW; 1F185A91B239A233 CRC64;
MAKLKLTELV LRDAHQSLLA TRMRLDDMLP IASKLDDAGY WSIESWGGAT FDSCIRYLGE
DPWERIRALK KAMPNTKQQM LLRGQNLLGY RHYADDVVEK FVERAHKNGV DVFRIFDAMN
DVRNLETAIK AAVKVGAHAQ GTISYTVSPV HTLDMWLTLA KQLEELGCHS ICIKDMAGLL
KPYDAEELIK ALKETVSIPI AMQCHATTGL STATYQKAID AGIDMLDTAI SSMSMTYGHS
ATETIVAIVE GTARDTELDL NQLEEIAAYF RDVRKKYAAF EGSLKGVDGR ILLAQVPGGM
LTNMENQLKE QGAADKLNEV LLEIPRVRED LGFIPLVTPT SQIVGTQAVL NVLTGERYKT
ITKETAGVLK GEYGLTPAPM NKELQERVLD GSDVITCRPA DNIAPELETL EAELLKEAQE
QGLTLADDKI DDVLTYALFP QVGLKFIKNR NNPDAFEPVP SVEDNSSKSP AKVSAKGNNV
KAEQYSVKVD GKVYDVVVAQ GGELKEVTLK DSEHLPQSAS VASGETLNAP LAGNIFKIKV
KAGQVVNEGD VVVIMEAMKM ETEVRAMHTG TIAEVLVSEG DSVTTGDAII ALA
//
