DCOA_KLEPN
ID DCOA_KLEPN Reviewed; 596 AA.
AC P13187;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Oxaloacetate decarboxylase alpha chain;
DE EC=7.2.4.2;
GN Name=oadA;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2454915; DOI=10.1016/s0021-9258(19)81564-8;
RA Schwarz E., Oesterhelt D., Reinke H., Beyreuther K., Dimroth P.;
RT "The sodium ion translocating oxalacetate decarboxylase of Klebsiella
RT pneumoniae. Sequence of the biotin-containing alpha-subunit and
RT relationship to other biotin-containing enzymes.";
RL J. Biol. Chem. 263:9640-9645(1988).
CC -!- FUNCTION: Catalyzes the decarboxylation of oxaloacetate coupled to
CC Na(+) translocation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) +
CC pyruvate; Xref=Rhea:RHEA:57724, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:29101; EC=7.2.4.2;
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC -!- SUBUNIT: Composed of three chains (alpha, beta, and gamma).
CC {ECO:0000250}.
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DR EMBL; J03885; AAA25120.1; -; Genomic_DNA.
DR PIR; A28088; A28088.
DR RefSeq; WP_004222624.1; NZ_WVHM01000014.1.
DR PDB; 6ROJ; EM; 2.90 A; A=508-593.
DR PDBsum; 6ROJ; -.
DR AlphaFoldDB; P13187; -.
DR SMR; P13187; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0015451; F:decarboxylation-driven active transmembrane transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 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 Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR01108; oadA; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biotin; Ion transport; Sodium; Sodium transport; Translocase;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..596
FT /note="Oxaloacetate decarboxylase alpha chain"
FT /id="PRO_0000146833"
FT DOMAIN 3..263
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 523..596
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 503..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 562
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 596 AA; 63534 MW; 284928FC45397054 CRC64;
MTVAITDVVL RDAHQSLFAT RLRLDDMLPV AAQLDDVGYR SLECWGGATF DACIRFLGED
PWVRLRELKK AMPKTPLQML LRGQNLLGYR HYADDVVERF VERAVKNGMD VFRVFDAMND
PRNMQAALQA VRRHGAHAQG TLSYTTSPAH TLQTWLDLTE QLLETGVDSV AIKDMSGILT
PHAAFELVSE IKKRYDVTLH LHCHATTGMA EMALLKAIEA GVDGVDTAIS SMSATYGHPA
TEALVATLAG TPYDTGLDIH KLESIAAYFR EVRKKYHAFE GQLKGTDSRI LVAQVPGGML
TNLEGQLKQQ SAAHRLDEVL AEIPRVREDL GFIPLVTPTS QIVGTQAVLN VLTGERYKTI
AKETAGILKG EYGRTPAPVN AALQARVLDG ADPVTCRPAD LLKPELAQLE ADVRRQAQEK
GITLAENAID DVLTVALFPQ PGLKFLENRH NPAAFEPVPQ AEAAQPVAKA EKPAASGVYT
VEVEGKAFVV KVSDGGDVSQ LTAAAPAPAP APAPASAPAA AAPAGAGTPV TAPLAGTIWK
VLASEGQTVA AGEVLLILEA MKMETEIRAA QAGTVRGIAV KAGDAVAVGD TLMTLA