ID G9YC28_HAFAL Unreviewed; 594 AA.
AC G9YC28;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Gluconate 2-dehydrogenase flavoprotein {ECO:0000313|EMBL:EHM39018.1};
GN ORFNames=HMPREF0454_04154 {ECO:0000313|EMBL:EHM39018.1};
OS Hafnia alvei ATCC 51873.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM39018.1, ECO:0000313|Proteomes:UP000005959};
RN [1] {ECO:0000313|EMBL:EHM39018.1, ECO:0000313|Proteomes:UP000005959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM39018.1,
RC ECO:0000313|Proteomes:UP000005959};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHM39018.1}.
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DR EMBL; AGCI01000099; EHM39018.1; -; Genomic_DNA.
DR RefSeq; WP_004095925.1; NZ_JH417552.1.
DR AlphaFoldDB; G9YC28; -.
DR GeneID; 69638035; -.
DR PATRIC; fig|1002364.3.peg.3731; -.
DR HOGENOM; CLU_008878_2_0_6; -.
DR Proteomes; UP000005959; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 146..348
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 450..573
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 594 AA; 65543 MW; 20F71F70519F8496 CRC64;
MANTMKKVDA VVVGFGWAGS IMAKELTEAG LNVVVLERGP HRDTYPDGAY PQVIDELTYN
IRRKLFQDLS KSTVTIRHNA SQTALPYRQL AAFLPGTGTG GAGLHWSGVH FRIDPMELRM
RSHYEERYGK NFIPEGMTIQ DFGVTYEELE PYFDKAEKVF GTSGTPWSVK GKVVGQGKGG
NPFAPDRSDN FPLPAQKRTF SAQMFAQAAE SVGYHPYDLP SANTSGPYTN TYGAQMGPCN
FCGFCSGYAC YMYSKASPNV NVWPALRQEP KFELRTNSHV LRVNLTDDKK RATGVTYVDA
QGRQVEQPAD LVILAAFQFH NVHLMLLSGI GKPYNPITNE GVVGRNFAYQ NISTIKAFFN
KDIFTNTFIG AGGAGVGVDD FNADNFDHAK YGFVGGSPFW VNQAGTKPIS GLPTRPGTPT
WGSKWKAEVA DVYSHHVSMD AHGAHQSYRA NYLDLDPNYK DVYGQPLLRM TFDWQENDIK
MSQFMHGRMH KIAEAMNPTV ISGSPKSEGT HFDTTVYQTT HMNGGAIMGE DPKTSAINRY
LQSWDVPNVF VPGASAFPQG LGYNPTGTLA ALTYWSARAI REQYLKNPGP LVQA
//
