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Database: UniProt
Entry: A0A060NK14_9BURK
LinkDB: A0A060NK14_9BURK
Original site: A0A060NK14_9BURK 
ID   A0A060NK14_9BURK        Unreviewed;       543 AA.
AC   A0A060NK14;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Choline dehydrogenase and related flavoprotein {ECO:0000313|EMBL:BAO81987.1};
GN   ORFNames=SRAA_2133 {ECO:0000313|EMBL:BAO81987.1};
OS   Serpentinimonas raichei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Serpentinimonas.
OX   NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO81987.1, ECO:0000313|Proteomes:UP000067461};
RN   [1] {ECO:0000313|EMBL:BAO81987.1, ECO:0000313|Proteomes:UP000067461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1 {ECO:0000313|EMBL:BAO81987.1,
RC   ECO:0000313|Proteomes:UP000067461};
RX   PubMed=24845058; DOI=10.1038/ncomms4900;
RA   Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA   Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA   Nealson K.H.;
RT   "Physiological and genomic features of highly alkaliphilic hydrogen-
RT   utilizing Betaproteobacteria from a continental serpentinizing site.";
RL   Nat. Commun. 5:3900-3900(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; AP014568; BAO81987.1; -; Genomic_DNA.
DR   RefSeq; WP_045532649.1; NZ_AP014568.1.
DR   AlphaFoldDB; A0A060NK14; -.
DR   STRING; 1458425.SRAA_2133; -.
DR   KEGG; cbaa:SRAA_2133; -.
DR   HOGENOM; CLU_002865_7_1_4; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000067461; Chromosome.
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|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067461}.
FT   DOMAIN          90..113
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          267..281
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   543 AA;  58881 MW;  2D52C32C6D4DA0E2 CRC64;
     MTPNPPTDAF DYLIVGGGSA GCVLAARLSA DPAVTVALLE AGGDGRDLAI RLPAGVVAML
     PARPFKYNNW AFETVPQPGL LGRCGYQPRG KALGGSSAIN AMLYARGHRS DYDDWAAAGA
     AGWSHAEVLP FFMRSEHNQR GPSAWRGVGG PLHVADQVSP RPIAQAFIEA CAQHGIAPNP
     DYNGEEQEGA YLFQVTQFHD AARRGQRCSA AAAFLHPVLQ RPNLTVLTHT QATRVLFEGR
     RAVGVQARQR GRHISLRARR EVVLCAGALQ SPQLLLLSGV GPPDELQRHG IPLVHRLPGV
     GQNLQDHLDL TLSYRSTRTD LFGIGFGAAW QHWQAWRQWR RDGSGPLSSP SAEGGAFWRS
     DAQQPRPDLQ LHFCVGIVDD HARKLHWGYG FSCHVCVLRP HARGRVGLRS ADPLAAPLID
     PAFLSDARDL HLLSRGAQQM REILLRSPLQ PWRGTPLYDE QLHGDAAWEQ LIRSRADTIY
     HPVGTCRMGV DEGAVVDAQL RVHGLQGLRV ADASIMPTLI GGNTNAPAIM IGERAAAWLL
     AAG
//
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