ID A0A1G0NBY0_9PROT Unreviewed; 616 AA.
AC A0A1G0NBY0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Oxaloacetate decarboxylase subunit alpha {ECO:0000313|EMBL:OGU20939.1};
GN ORFNames=A2580_02505 {ECO:0000313|EMBL:OGU20939.1};
OS Hydrogenophilales bacterium RIFOXYD1_FULL_62_11.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1798415 {ECO:0000313|EMBL:OGU20939.1, ECO:0000313|Proteomes:UP000179278};
RN [1] {ECO:0000313|EMBL:OGU20939.1, ECO:0000313|Proteomes:UP000179278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGU20939.1}.
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DR EMBL; MGZO01000106; OGU20939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0NBY0; -.
DR Proteomes; UP000179278; 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}.
FT DOMAIN 4..264
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 539..614
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 518..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 66750 MW; A4D945AF947A8E98 CRC64;
MAKVFVTDLV LRDGHQSLIA TRMRTEDMLP ICSKLDQVGF WSLEAWGGAT FDACVRFLRE
DPWQRLRQLR KALPNTRIQM LLRGQNLLGY RNYSDDVVRA FVQKSADNGV DVFRIFDAMN
DLRNLQVSVE AVKAAGKHAE GTVCYTTSPV HNIPHFVELA KGLAEMGCDT IAIKDMAGLL
TPYTAFELVG AIRAATNLPV HTHSHATSGL AHMTHLKAIE AGATIIDTCV GAFAEGASHP
TTQSLVAALA GTQYDTGLSL PLIEEISAYF KETRKKYWQY ESAFTGTDTR VLINQVPGGM
ISNLANQLKE QGALDKMDAV LEEIPRVRED LGYPPLVTPT SQIVGTQAAL NVMTGARYKS
VTNEVKLYLQ GRYGRAPGHI NEEVRKIAIG DLNITTCRPA DLLGDELDKL RGEIEGLAKS
DEDVLTYAMF PEIGKTWLQE RAAGSLKPEQ LLPQGTSQQD SAPRYAADEF KITLHGETYH
IKLSGSGRSD ATQRPYFVSI DGVTEEVLVE PLNEVAVASS GDNAPRKGKA TASAAPGQKP
HASHPGHVTA AMPGTIVDVL VSIGQVVKAG DGILVIEAMK MENEVQAPIA GIVISIFAKK
GDAVTPDMAL VEIQPE
//
