GenomeNet

Database: UniProt
Entry: A0A0F5AS22_9GAMM
LinkDB: A0A0F5AS22_9GAMM
Original site: A0A0F5AS22_9GAMM 
ID   A0A0F5AS22_9GAMM        Unreviewed;       563 AA.
AC   A0A0F5AS22;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=WN56_00130 {ECO:0000313|EMBL:KKA45589.1};
OS   Salinivibrio sp. KP-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Salinivibrio.
OX   NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA45589.1, ECO:0000313|Proteomes:UP000033449};
RN   [1] {ECO:0000313|EMBL:KKA45589.1, ECO:0000313|Proteomes:UP000033449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KP-1 {ECO:0000313|EMBL:KKA45589.1,
RC   ECO:0000313|Proteomes:UP000033449};
RA   Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA   Kaur N., Bala M., Mayilraj S.;
RT   "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT   nov., a novel halotolerant gammaproteobacterium isolated from marine
RT   sediment and emended description of the genus Salinivibrio.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         ChEBI:CHEBI:17499; EC=1.1.99.1;
CC         Evidence={ECO:0000256|RuleBase:RU003969};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC       route): step 1/1. {ECO:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:KKA45589.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LAQR01000001; KKA45589.1; -; Genomic_DNA.
DR   RefSeq; WP_046073047.1; NZ_LAQR01000001.1.
DR   AlphaFoldDB; A0A0F5AS22; -.
DR   PATRIC; fig|1406902.3.peg.27; -.
DR   OrthoDB; 9785276at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000033449; Unassembled WGS sequence.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
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; IPR011533; BetA.
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   NCBIfam; TIGR01810; betA; 1.
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:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KKA45589.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033449}.
FT   DOMAIN          86..109
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          258..272
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         88
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   563 AA;  62734 MW;  F228C5706E77A55A CRC64;
     MGQQQNYDYI IVGAGSAGCV LANRLSANPD NNVLLLEAGR PDYRLDFRIH MPAALTYLLT
     DSTYNWLYES EPEPNMHNRR IAQPRGKVLG GSSSINGMIY IRGNALDYEK WANEHGLKTW
     DYAHCLPYFR KCETRLAGQN DYHGNNGPLA VTTAKCDNPL FSAFFDATQQ AGYPLTDDVN
     GYQQEGFGIF DQNIYRGRRH SAARAYLHPV MNRKNLTVIT GATTDKVLFE NKTAMGVEYR
     KWGRTKTAYG AEIISCGGAI NSPKLLQLSG IGDETMLKNL GVKPVHHLPG VGENLQDHLE
     LYVQYECKEP VSMYPALKFH NQPKIGFDWL FRRKGAAATN HFEAGGFVRG NDEVAYPNLQ
     FHFLPLAIRY DGSAPNKGHG FQLHVGPMNT DVRGHVKIRS TNPDEKPEIF FNYLSTPQER
     KEWVEAIRVS RDIIAQPAFD HLRGKELSPG SAAQTDQEIL DFVAREGESA YHPSCTCKMG
     LASDEMAVVD ESLKVHGVNN LRVVDASVFP AITNGNLYAP TIMVAEKAAD MIMGHTLSPA
     KDAEYYRYLP DHTPAPEKDA ALV
//
DBGET integrated database retrieval system