ID E1ST15_FERBD Unreviewed; 597 AA.
AC E1ST15;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Oxaloacetate decarboxylase alpha subunit {ECO:0000313|EMBL:ADN75071.1};
GN OrderedLocusNames=Fbal_0862 {ECO:0000313|EMBL:ADN75071.1};
OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN75071.1, ECO:0000313|Proteomes:UP000006683};
RN [1] {ECO:0000313|EMBL:ADN75071.1, ECO:0000313|Proteomes:UP000006683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC {ECO:0000313|Proteomes:UP000006683};
RX DOI=10.4056/sigs.1161239;
RA Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL Stand. Genomic Sci. 3:174-182(2010).
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DR EMBL; CP002209; ADN75071.1; -; Genomic_DNA.
DR RefSeq; WP_013344377.1; NC_014541.1.
DR AlphaFoldDB; E1ST15; -.
DR STRING; 550540.Fbal_0862; -.
DR GeneID; 67181111; -.
DR KEGG; fbl:Fbal_0862; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_3_6; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000006683; 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:UP000006683}.
FT DOMAIN 6..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 518..597
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 597 AA; 64022 MW; E9CDE98CAD0DBA3B CRC64;
MTATPLALTD VVLRDAHQSL LATRLRLDDM LPAAEQLDRV GYWSLESWGG ATFDACIRYL
GEDPWYRIRA LKEAMPNTPQ QMLLRGQNLL GYRHYADDVV EAFVQRAYAS GVEVFRIFDA
LNDTRNLETA IRAVNAAGGH AQGTLSYTTS PVHTLESWVE LAKEQAALGC QSLCIKDMAG
LLTPTAAFEL ITTLKSEVGL PIAMQCHATT GLSTATYQKA IEAGIDVLDT AISSMSMTYG
HTATETVMAM VAGTDRDTGL DPAQLAPIAQ HFRQVRSRYA EFEGSLRGVD ARILTAQVPG
GMLTNMENQL KEQGALDRLD EVLEEIPRVR EELGFLPLVT PTSQIVGTQA VLNILTGERY
KSITKETQGV LRGEYGRTPA PVDAELQARV LDGQAPVTGR PADDLAPELN RLTETVTQLA
QSDGFTLADS AIDDVLTYAL FPQIGRKFLM NRGNPDAFEP APGQAKAAKP VATEAPVQPA
SRGPATYQVR VDGRSYSVEV SEGGEIGQIQ PQPAASATPT QPTPAPVASV VSAPLAGNVF
KVLIGPGQTV AEGDVVLVME AMKMETEIRA SSAGQVQQLH VREGDAVSVG DPLVSLS
//