ID A0A1N7RX08_9BURK Unreviewed; 446 AA.
AC A0A1N7RX08;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Gluconate 2-dehydrogenase (Acceptor) {ECO:0000313|EMBL:SIT39643.1};
DE EC=1.1.99.3 {ECO:0000313|EMBL:SIT39643.1};
GN ORFNames=BN2476_230135 {ECO:0000313|EMBL:SIT39643.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT39643.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT39643.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT39643.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR000018-50};
CC Note=Binds 3 heme c groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000018-50};
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DR EMBL; CYGY02000023; SIT39643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7RX08; -.
DR OrthoDB; 9809720at2; -.
DR Proteomes; UP000195569; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; Cytochrome c-like domain; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR PANTHER; PTHR35008:SF8; BLL4482 PROTEIN; 1.
DR PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR Pfam; PF00034; Cytochrom_C; 3.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR SUPFAM; SSF46626; Cytochrome c; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000018-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000018-51};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000018-51};
KW Oxidoreductase {ECO:0000313|EMBL:SIT39643.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..46
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 47..446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012071626"
FT DOMAIN 63..166
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 208..318
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 335..425
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 77
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 80
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 81
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:0000256|PIRSR:PIRSR000018-51"
FT BINDING 223
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 226
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 227
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:0000256|PIRSR:PIRSR000018-51"
FT BINDING 348
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 351
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 352
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:0000256|PIRSR:PIRSR000018-51"
SQ SEQUENCE 446 AA; 48506 MW; 83C7A5998BF9FA27 CRC64;
MKTLSSRSVN RMQRAARITR RATISLVAGT ALALAAIAPQ SPFVSAAYGA GAATPAAAGA
RPEQVVRGEY LARAGDCVAC HTAPRGKTFG GGLAMETPFG TLYTPNISPD NEYGIGKWTA
DDFFKMMRTG KSPDGKLIYP AMPIAQYTKV TREDSDAIFA YLKSVEPVHQ ANRKHALRFP
FNQRELLIGW RSLYFREGEF QPNPTRSVEW NRGAYLVEGL GHCTMCHTKI NLLGGSSKSE
QFAGGLIPVQ NWYAPSLTSD KDGGLGDWSI KDIVDLLQAG ISDRGAVYGP MAEVTYHSLQ
YMTDDDVKAM AVYLKTLPDN DPGRKTGPSA TVKPAVFESG QHIYMTKCAM CHGDNGEGKL
QHYPPLARNQ SIEMDSAVNP IRIVLNGGFP PGTRRNPEPY GMPPFAQELN DADAAAVVTY
IRTAWGNHGQ PVTAKQVNEL RKAPLH
//