ID A3D1D6_SHEB5 Unreviewed; 606 AA.
AC A3D1D6;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Oxaloacetate decarboxylase alpha subunit {ECO:0000313|EMBL:ABN60549.1};
GN OrderedLocusNames=Sbal_1025 {ECO:0000313|EMBL:ABN60549.1};
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN60549.1, ECO:0000313|Proteomes:UP000001557};
RN [1] {ECO:0000313|EMBL:ABN60549.1, ECO:0000313|Proteomes:UP000001557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000563; ABN60549.1; -; Genomic_DNA.
DR RefSeq; WP_011846058.1; NC_009052.1.
DR AlphaFoldDB; A3D1D6; -.
DR STRING; 325240.Sbal_1025; -.
DR KEGG; sbl:Sbal_1025; -.
DR HOGENOM; CLU_000395_4_3_6; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000001557; 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 15..275
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 533..606
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 606 AA; 66213 MW; 19A4E9758EE9A0DA CRC64;
MTFVSNSTTA VAKPLFLTDV VLRDAHQSIL ATRLRIDDML PIAPLLDKIG FWSLESWGGA
TFDACIRYLG EDPWDRIREL KKAMPNTPQQ MLLRGQNLLG YRHYADDLVT RFVERAHTNG
VDVFRIFDAM NDVRNLETAV KAVRQVGGHA QGTISYTTSP VHTIETWVDM AKRLEDMGCD
SLCIKDMAGL LKPMEAFELI SRLKSQTQLV LSMHCHATTG LSTATYQKAI EAGIDVLDTA
ISSMSQTYGH TATETVIAMV EDTERATGYD MVLLEEIAAY FREVRKKYAK FEGALKGIDS
RILRAQVPGG MLTNMESQLK EQGAADKMDL VLEEIPRVRA DLGFLPLVTP TSQIVGSQAV
INVLMGERYK SLTKETEGVL KGEYGATPAP VDAALQARVL QGAEAITCRP ADLLTPELAK
LRLELADKAQ EQGIRLSSEH DDDVLTYALF PQIGLQFLKN RDDPSAFEPK PEVTAALATN
AADRGQTYTV TVEGQEYVVE VAAGGDISQI QPQGQSVHAV QTATASTMPT ACHGEIRLEM
SAPLSGNIFK VHVSPGDRVC EGDVVIILEA MKMETEIRAQ GDGIIAKLWV KEGDSVSVGS
QLLALA
//
