ID A0A238IXS1_9RHOB Unreviewed; 531 AA.
AC A0A238IXS1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Alcohol dehydrogenase [acceptor] {ECO:0000313|EMBL:SMX22474.1};
DE EC=1.1.99.- {ECO:0000313|EMBL:SMX22474.1};
GN Name=alkJ_1 {ECO:0000313|EMBL:SMX22474.1};
GN ORFNames=BOA8489_00571 {ECO:0000313|EMBL:SMX22474.1};
OS Boseongicola aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Boseongicola.
OX NCBI_TaxID=1470561 {ECO:0000313|EMBL:SMX22474.1, ECO:0000313|Proteomes:UP000201838};
RN [1] {ECO:0000313|EMBL:SMX22474.1, ECO:0000313|Proteomes:UP000201838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8489 {ECO:0000313|EMBL:SMX22474.1,
RC ECO:0000313|Proteomes:UP000201838};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; FXXQ01000001; SMX22474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238IXS1; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000201838; 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; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000313|EMBL:SMX22474.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000201838}.
FT DOMAIN 80..103
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 253..267
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 531 AA; 57763 MW; 122393ADB15AC35C CRC64;
MEADYVVIGA GSAGCVVANR LSADPSVKVV LLEAGPVDRN PWIHIPVGYF KTMHNPTVDW
CYRTEPDPGL NGRSIDWPRG KVLGGSSSLN GLLYVRGQAQ DYDRWRQMGN TGWGWDDVLP
LFKRAEANER GADEFHGDDG PLAVSNMRIQ RPICDAWVAA AQTAGYPFNP DYNGSTQEGV
GYFQLTTKNG RRCSAAVAYL KPVRHRENLK IVTNALVSKV NIENKRAVSV TYRDSGGSEK
VVAARREIVL SGGAINSPQI LMLSGIGDAE QLKANGVEVV HDLPGVGKNL QDHLQARLVF
KCNEATLNDE VRSLFNQARI ALKYAMFRSG PMTMAASLAT GFLKTRDDVV TPDIQFHVQP
WSADSPGAGV HPFSAFTMSV CQLRPESRGE IRLDGPSPKS YPKIHPNYLS TETDCRTIVE
GVNIARRIAR EAPLNSKIAE AFRPDDTLAV DDYEGTLDWA RNNSVSIYHP AGTCKMGSGT
EAVVDAELKV HGIEGLRVAD CSIMPEIVSG NTNAPAIMIG EKVSDLMGAR V
//
