ID V2Y0Q3_9FIRM Unreviewed; 651 AA.
AC V2Y0Q3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Oxaloacetate decarboxylase alpha chain {ECO:0000313|EMBL:USF28059.1};
DE SubName: Full=Oxaloacetate decarboxylase alpha subunit {ECO:0000313|EMBL:ESL15554.1};
GN Name=oadA {ECO:0000313|EMBL:USF28059.1};
GN ORFNames=N510_00187 {ECO:0000313|EMBL:ESL15554.1}, N510_003017
GN {ECO:0000313|EMBL:USF28059.1};
OS Firmicutes bacterium ASF500.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL15554.1};
RN [1] {ECO:0000313|EMBL:ESL15554.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL15554.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF28059.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF500 {ECO:0000313|EMBL:USF28059.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AYJP01000003; ESL15554.1; -; Genomic_DNA.
DR EMBL; CP097573; USF28059.1; -; Genomic_DNA.
DR AlphaFoldDB; V2Y0Q3; -.
DR STRING; 1378168.N510_00187; -.
DR PATRIC; fig|1378168.3.peg.192; -.
DR eggNOG; COG4770; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_3_9; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000017395; Chromosome.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
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:UP000017395}.
FT DOMAIN 7..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 572..651
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 651 AA; 69460 MW; A6808817DCB9DC93 CRC64;
MSKTRKVGFT ETVLRDANQS LIATRLPYSK FEPILETMDK AGYYSAEVWG GATFDVCLRY
LQEDPWERLR KIRAKMPNTK LQMLLRGQNI LGYKHYPDDV VRKFVEHSIK NGIDIIRIFD
ALNDARNLQV AIEETVKRGG HASGTICFTT SPVHTLEKNV QMVKELKQMG VKSICIKDMA
GIMGPKESYD LVSAIKDAVP ELPLVIHTHC TTGLAFMTCL KGVEAGADVI DTAISPMSGG
TAQPATETLA YALRSLGYQV DLDDKVLIQM ADFFKGVRAD FIKDGTLDPI SMATDTQCLN
YQIPGGMLSN LISQLKMMNA IDKLDQALAE TPKVRADLGY PPLVTPTSQM VGSQAVQNVL
AGERYKVVGK EIKAYCRGEY GRTPAPIDPS IQKKILGSTP VVEGRFADSL EPEFEKTKKE
LGATAKCDED VLSYIAFPQV AMAFFKDREA GFPKKADPAK PAAAPAAKKE SDLPPVPAWQ
GHVYYTNIPA SLSNGVNARP IQPFAASYQP PHLVMGSRDT CPGTYTITID GKAYAVSVAA
ADGPAPAAAP APVAVAAPAP VAAPAPAAAP APAAAPAPAA GETAVKSPMP GNIFKVECKP
GQAVKAGDVL VVLEAMKMEI EVSAPADGTV KSVAATVGTA VNTDDLLVVL G
//
