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Database: UniProt
Entry: A8HRG4_AZOC5
LinkDB: A8HRG4_AZOC5
Original site: A8HRG4_AZOC5 
ID   A8HRG4_AZOC5            Unreviewed;       562 AA.
AC   A8HRG4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   OrderedLocusNames=AZC_1183 {ECO:0000313|EMBL:BAF87181.1};
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF87181.1, ECO:0000313|Proteomes:UP000000270};
RN   [1] {ECO:0000313|EMBL:BAF87181.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=17720818; DOI=10.1128/AEM.01514-07;
RA   Suzuki S., Aono T., Lee KB., Suzuki T., Liu CT., Miwa H., Wakao S., Iki T.,
RA   Oyaizu H.;
RT   "Rhizobial factors required for stem nodule maturation and maintenance in
RT   Sesbania rostrata-Azorhizobium caulinodans ORS571 symbiosis.";
RL   Appl. Environ. Microbiol. 73:6650-6659(2007).
RN   [2] {ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAF87181.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=18522759; DOI=10.1186/1471-2164-9-271;
RA   Lee KB., Backer P.D., Aono T., Liu CT., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T.T., Ussery D.W., D'Haeze W., Herder J.D., Gevers D.,
RA   Vereecke D., Holsters M., Oyaizu H.;
RT   "The genome of the versatile nitrogen fixer Azorhizobium caulinodans
RT   ORS571.";
RL   BMC Genomics 9:271-271(2008).
RN   [4] {ECO:0000313|EMBL:BAF87181.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=19542345; DOI=10.1128/AEM.00398-09;
RA   Tsukada S., Aono T., Akiba N., Lee KB., Liu CT., Toyazaki H., Oyaizu H.;
RT   "Comparative genome-wide transcriptional profiling of Azorhizobium
RT   caulinodans ORS571 grown under free-living and symbiotic conditions.";
RL   Appl. Environ. Microbiol. 75:5037-5046(2009).
RN   [5] {ECO:0000313|EMBL:BAF87181.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=20382809; DOI=10.1128/AEM.00238-10;
RA   Akiba N., Aono T., Toyazaki H., Sato S., Oyaizu H.;
RT   "phrR-like gene praR of Azorhizobium caulinodans ORS571 is essential for
RT   symbiosis with Sesbania rostrata and is involved in expression of reb
RT   genes.";
RL   Appl. Environ. Microbiol. 76:3475-3485(2010).
RN   [6] {ECO:0000313|EMBL:BAF87181.1, ECO:0000313|Proteomes:UP000000270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC   NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX   PubMed=21571889; DOI=10.1128/AEM.02327-10;
RA   Liu CT., Lee KB., Wang YS., Peng MH., Lee KT., Suzuki S., Suzuki T.,
RA   Oyaizu H.;
RT   "Involvement of the azorhizobial chromosome partition gene (parA) in the
RT   onset of bacteroid differentiation during Sesbania rostrata stem nodule
RT   development.";
RL   Appl. Environ. Microbiol. 77:4371-4382(2011).
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}.
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DR   EMBL; AP009384; BAF87181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8HRG4; -.
DR   STRING; 438753.AZC_1183; -.
DR   KEGG; azc:AZC_1183; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_5; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000000270; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000000270}.
FT   DOMAIN          92..115
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          264..278
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         94
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         102..105
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   562 AA;  61378 MW;  59F8ABEFB370E002 CRC64;
     MMERTVASPA SPAIFDYVIV GSGSAGAVLA DRLSADGRFT VHVLEYGGSD RSLLIQMPAA
     LSIPMNMPKY NWGFETEPEP GLGGRRLVCP RGKVIGGSSS VNGMVYVRGN PHDFDRWEEE
     GAQGWGYRHV LPYFQRAESR QEGGDAYRGA TGPLATRYGP LENPLYNVFV EAARQAGYPA
     TSDINGAQQE GFGRMDMTVK DGVRWSTANA YLKPALKRPN LSLETHALVL AVELEGRRAV
     GVRYERDGTE QIVKASREVI LAAGPINSPK LLKLSGIGPA QELADLGIPV VADRPGVGEN
     LQDHLEFYFQ VACTQPITLY SKTGLLSRGL VGAQWLLARS GLGASNHFES CGFIRSRAGI
     RYPDIQYHFL PLAVSYDGKG LASEHGFQAH VGPMRSKSRG WVRLRSRDAR EHPRIFFNYL
     GHEDDITEMR ACVRLTREIF AQAAFDPYRG REIQPGADVT SDEAIDAFVR EKVESAYHPS
     CSCRMGRADD PMAVVTPDTK VIGIEGLRVV DSSIMPSVTT GNLNAPTIMI GEKASDIILG
     KPALAASNAP YYTAENWRTA QR
//
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