ID   GADH3_PANCY             Reviewed;         220 AA.
AC   O34213;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   13-SEP-2023, entry version 64.
DE   RecName: Full=Gluconate 2-dehydrogenase subunit 3;
DE            Short=GA 2-DH subunit 3;
DE            Short=GADH subunit 3;
DE            EC=1.1.99.3;
DE   Flags: Precursor;
OS   Pantoea cypripedii (Pectobacterium cypripedii) (Erwinia cypripedii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=55209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 43-57, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 29267 / DSM 3873 / CIP 105195 / LMG 2657 / NCPPB 3004;
RX   PubMed=9352901; DOI=10.1128/jb.179.21.6566-6572.1997;
RA   Yum D.-Y., Lee Y.-P., Pan J.-G.;
RT   "Cloning and expression of a gene cluster encoding three subunits of
RT   membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267
RT   in Escherichia coli.";
RL   J. Bacteriol. 179:6566-6572(1997).
CC   -!- FUNCTION: Part of the heterotrimer that catalyzes the conversion of D-
CC       gluconate to 2-dehydro-D-gluconate. The role of this subunit in the
CC       heterotrimer is not known.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + D-gluconate = 2-dehydro-D-gluconate + AH2;
CC         Xref=Rhea:RHEA:12769, ChEBI:CHEBI:13193, ChEBI:CHEBI:16808,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:18391; EC=1.1.99.3;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:9352901};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:9352901};
CC   -!- SUBUNIT: Heterotrimer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
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DR   EMBL; U97665; AAC45883.1; -; Genomic_DNA.
DR   PIR; A38575; A38575.
DR   AlphaFoldDB; O34213; -.
DR   SMR; O34213; -.
DR   STRING; 55209.HA50_01495; -.
DR   BioCyc; MetaCyc:MONOMER-18007; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033717; F:gluconate 2-dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   InterPro; IPR027056; Gluconate_2DH_su3.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF13618; Gluconate_2-dh3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Membrane; Oxidoreductase; Signal.
FT   SIGNAL          1..42
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:9352901"
FT   CHAIN           43..220
FT                   /note="Gluconate 2-dehydrogenase subunit 3"
FT                   /id="PRO_0000045856"
SQ   SEQUENCE   220 AA;  24368 MW;  CDDB85B110663803 CRC64;
     MSEHKNGHTR RDFLLRTITL APAMAVGSTA MGALVAPMAA GAAEQSSGSQ TARDYQPTWF
     TAEEFAFITA AVARLIPNDE RGPGALEAGV PEFIDRQMNT PYALGSNWYM QGPFNPDLPK
     ELGYQLPLVP QQIYRLGLAD ADSWSKHQHG KVFAELSGDQ QDALLSDFES GKAEFTQLPA
     KTFFSFLLQN TREGYFTRSD PRWQSGHGGL EADWLPRRTR
//