ID A0A3G3INM3_9GAMM Unreviewed; 610 AA.
AC A0A3G3INM3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Oxaloacetate decarboxylase alpha subunit {ECO:0000313|EMBL:AYQ57400.1};
GN ORFNames=MS2017_1726 {ECO:0000313|EMBL:AYQ57400.1};
OS Bathymodiolus thermophilus thioautotrophic gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2360 {ECO:0000313|EMBL:AYQ57400.1, ECO:0000313|Proteomes:UP000278334};
RN [1] {ECO:0000313|EMBL:AYQ57400.1, ECO:0000313|Proteomes:UP000278334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR9N {ECO:0000313|EMBL:AYQ57400.1,
RC ECO:0000313|Proteomes:UP000278334};
RA Won Y.-J.;
RT "Genome sequence of the bacterial symbiont EPR9N from a vent mussel
RT Bathymodiolus thermophilus.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP024634; AYQ57400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3INM3; -.
DR KEGG; bthg:MS2017_1726; -.
DR Proteomes; UP000278334; 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 21..281
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 541..610
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 610 AA; 66890 MW; 45E03D987D22B28B CRC64;
MLDFLKNVVQ KPDNQKNTKK VEITELVFRD AHQSLFATRM RIDDMLPIAD KLDKIGYWSM
ESWGGATFDS CIRYLGEDPW DRIREIKAVM PNTPQQMLLR GQNLLGYRHY SDDVVRKFID
RCAENGVSVF RIFDAMNDMR NLKTAVDQTV KLGQHAQGTI SYTVSPVHTM QTWVDMAKAI
EDMGAHSLCI KDMAGLLHPY DAYDLVKKLK ATVDIPIQLH AHATTGLSTA SIVKAVEAGI
DRVDTAIGSM SMTYGHSATN SVVAILENSP RKTGLDLEKL EEIDAYFRPI RAKYAQFEGS
LKGVDSRILL SQVPGGMLTN MESQLREQNA IDKMDEVMAE IPRVRKDLGY IPLVTPTSQI
VGTQSVLNVL TGERYKTITK ESAGILKGEY GATPAPVDQA LQIKVLDGGE PITCRPADNI
APEMNILEQE FDKIVAEKGL TVADDKIDDL LTYALFPQVG INFIKNRNNA EFFESVPEAG
NSVNNSTEEG SYTVSFKGTS YKVDVSAGGN ITSMKSASDA TVSATTPAKK EMIEKLPAAG
TEDIGAPLSG NIWKVMVLPH QKINEGDVLV ILEAMKMETE IKAARGGVVA SVSVKEGDAV
TVGQTLLSMV
//