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Entry: A0A0B5FDV9_9DELT
LinkDB: A0A0B5FDV9_9DELT
Original site: A0A0B5FDV9_9DELT 
ID   A0A0B5FDV9_9DELT        Unreviewed;       491 AA.
AC   A0A0B5FDV9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-APR-2018, entry version 19.
DE   SubName: Full=Betaine-aldehyde dehydrogenase {ECO:0000313|EMBL:AJF05478.1};
GN   ORFNames=GSUB_01250 {ECO:0000313|EMBL:AJF05478.1};
OS   Geoalkalibacter subterraneus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geoalkalibacter.
OX   NCBI_TaxID=483547 {ECO:0000313|EMBL:AJF05478.1, ECO:0000313|Proteomes:UP000035036};
RN   [1] {ECO:0000313|EMBL:AJF05478.1, ECO:0000313|Proteomes:UP000035036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red1 {ECO:0000313|EMBL:AJF05478.1,
RC   ECO:0000313|Proteomes:UP000035036};
RX   PubMed=25767222;
RA   Badalamenti J.P., Krajmalnik-Brown R., Torres C.I., Bond D.R.;
RT   "Genomes of Geoalkalibacter ferrihydriticus Z-0531T and
RT   Geoalkalibacter subterraneus Red1T, Two Haloalkaliphilic Metal-
RT   Reducing Deltaproteobacteria.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant
CC       glycine betaine. Catalyzes the reversible oxidation of betaine
CC       aldehyde to the corresponding acid.
CC       {ECO:0000256|SAAS:SAAS00630975}.
CC   -!- CATALYTIC ACTIVITY: Betaine aldehyde + NAD(+) + H(2)O = betaine +
CC       NADH. {ECO:0000256|SAAS:SAAS00630953}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|SAAS:SAAS00630937};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine from betaine aldehyde: step 1/1.
CC       {ECO:0000256|SAAS:SAAS00631176}.
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000256|SAAS:SAAS01033883}.
CC   -!- SUBUNIT: Dimer of dimers. {ECO:0000256|SAAS:SAAS00630970}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345, ECO:0000256|SAAS:SAAS00644510}.
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DR   EMBL; CP010311; AJF05478.1; -; Genomic_DNA.
DR   RefSeq; WP_040198824.1; NZ_CP010311.1.
DR   EnsemblBacteria; AJF05478; AJF05478; GSUB_01250.
DR   KEGG; gsb:GSUB_01250; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000035036; Chromosome.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR011264; BADH.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01804; BADH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000035036};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00631084};
KW   NAD {ECO:0000256|SAAS:SAAS00644501};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000256|SAAS:SAAS00644509};
KW   Potassium {ECO:0000256|SAAS:SAAS00630946};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035036}.
FT   DOMAIN       12    477       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   491 AA;  53879 MW;  97003E6243981C8B CRC64;
     MIEKRMYVDG QWVDARSGKT RSIINPANQE VIAEVAEGGR EDSRVAIAAA RRAFDQGDWP
     RTPANERGAL VYRLGELVAR EREELARLET LDTGKTLEES RWDMDDIAGI FKYYGGLADK
     DGGESIASPV PDSSSTLVRE PVGVCGQISP WNYPLLQASW KMAPALAAGC TIVMKPSEIT
     PLTTIRITEL AQEAGFPAGV VNTVLGEGAE VGAELAESPQ VDLISFTGGI TTGKQVMRAA
     SGNVKKVALE LGGKNPNIIF ADADFDTALD YVLNGVFFHA GQICSAGARV MVEEPLHDRL
     VEALAQRIKR IVVGDGFNPD SRMGPLISAE HRDKVERYVE VAQREGANLV LGGRRPEADH
     LQDGFYYEPT LFTGCSNDMK IVQEEVFGPV ITIEKFSTED EAVARANSTI YGLSAGFWTR
     DPDRIQRMSR ALRFGTVWVN DFNVYFTQAP WGGYKQSGLG RELGKMGLEE YTEVKHVYQN
     FNAKPLNWFG A
//
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