ID F2G424_ALTMD Unreviewed; 604 AA.
AC F2G424;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Oxaloacetate decarboxylase {ECO:0000313|EMBL:AEA97366.1};
GN OrderedLocusNames=MADE_1006120 {ECO:0000313|EMBL:AEA97366.1};
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373 {ECO:0000313|EMBL:AEA97366.1, ECO:0000313|Proteomes:UP000001870};
RN [1] {ECO:0000313|EMBL:AEA97366.1, ECO:0000313|Proteomes:UP000001870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype
RC {ECO:0000313|Proteomes:UP000001870};
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
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DR EMBL; CP001103; AEA97366.1; -; Genomic_DNA.
DR RefSeq; WP_012517708.1; NC_011138.3.
DR AlphaFoldDB; F2G424; -.
DR KEGG; amc:MADE_1006120; -.
DR HOGENOM; CLU_000395_4_3_6; -.
DR Proteomes; UP000001870; 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}.
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 529..604
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 455..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 65099 MW; 1C9328DB6EF340DC CRC64;
MSKPLALTEL VLRDAHQSLL ATRMRIEDML PIAEKLDKAG FWSVESWGGA TFDACIRYLG
EDPWERIRKL KAAMPNTKQQ MLLRGQNLLG YRHYADDVVT RFVERAHESG VDVFRIFDAM
NDIRNLKTAI KATIDSGAHA QGTISYTVSP VHNLKLWLDM AKQLEDLGVH SICIKDMAGL
LKPYECEALI TGLKETVSVP IAMQCHATTG LSTATYQKAV DAGIDMLDTA ISSMSMTYGH
TATETMVSIV EGTERDTGIA LPELEEIASY FRDVRKKYSK FEGSLKGVDA RILLAQVPGG
MLTNMESQLK EQGAEDKFEE VLKEIPRVRE DLGFIPLVTP TSQIVGTQSV LNVLTGERYK
SITKETAGVL KGEYGATAAP VNKALQERVL DGAEPVTCRP ADNIAPELDA LSKELDELAE
KKQLSLSDDK IDDVLTYALF PQIGLKFIEN RGNPDAFEPA PSAQSSQSAD VAQVEKTAAN
TSTSGSETYD VNVDGKVYHV EVAPSGTLTS VTPAGAAQSS APASASNTQA SASTSQSIDA
PLAGNVFKIL VKNGDSIAEG DVVMILEAMK METEIRAAFT GTVTEVTVGE GDAVSSGQPL
ILLG
//