GADH2_PANCY
ID GADH2_PANCY Reviewed; 441 AA.
AC O34215;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Gluconate 2-dehydrogenase cytochrome c subunit;
DE Short=GA 2-DH cytochrome c subunit;
DE Short=GADH cytochrome c subunit;
DE EC=1.1.99.3;
DE Flags: Precursor;
OS Pantoea cypripedii (Pectobacterium cypripedii) (Erwinia cypripedii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=55209;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-28, 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.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
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: Binds 3 heme c groupd covalently per subunit. {ECO:0000305}.
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DR EMBL; U97665; AAC45884.1; -; Genomic_DNA.
DR PIR; C38575; C38575.
DR AlphaFoldDB; O34215; -.
DR STRING; 55209.HA50_01505; -.
DR BioCyc; MetaCyc:MON-18006; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0033717; F:gluconate 2-dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; SSF46626; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Repeat; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:9352901"
FT CHAIN 20..441
FT /note="Gluconate 2-dehydrogenase cytochrome c subunit"
FT /id="PRO_0000045855"
FT DOMAIN 26..129
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 173..289
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 312..403
FT /note="Cytochrome c 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 40
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 43
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 44
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 188
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 191
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 192
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 325
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 328
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 329
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 441 AA; 47097 MW; 0AF512CFA99DA123 CRC64;
MMKSILALVL GTLSFAALAD DQANDALVKR GEYLARAGDC VACHSVKGGQ PFAGGLPMAT
PIGTIYSTNI TPDKTTGIGD YSYDDFQKAV RHGVAKNGDT LYPAMPYPSY AVVSDEDMKA
LYAYFMHGVA PVAQANKDSD IPWPLSMRWP LAIWRGVFAP DVKAFQPAAQ EDPVLARGRY
LVEGLGHCGA CHTPRSITMQ EKALSNDGAH DYLSGSSAPI DGWTASNLRG DNRDGLGRWS
EDDLRQFLRY GRNDHTAAFG GMTDVVEHSL QHLSDDDITA IARYLKSLGA KDASQTVFTQ
DDQVAKALWK GDDSQTGASV YVDSCAACHK TDGSRLSALL PGAAWQPGGA GEPDPTSLIH
IVLTGGTLPG VQGAPTAITM PAFGWRLNDQ QVADVVNFIR GSWGNGAKAT VTAKDVASLR
KDETVQAHQG NADIKVLEQQ Q
