ID A0A221MI30_9BACI Unreviewed; 485 AA.
AC A0A221MI30;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Betaine-aldehyde dehydrogenase {ECO:0000313|EMBL:ASN07262.1};
GN Name=betB {ECO:0000313|EMBL:ASN07262.1};
GN ORFNames=CFK40_01995 {ECO:0000313|EMBL:ASN07262.1};
OS Virgibacillus necropolis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN07262.1, ECO:0000313|Proteomes:UP000204391};
RN [1] {ECO:0000313|EMBL:ASN07262.1, ECO:0000313|Proteomes:UP000204391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN07262.1,
RC ECO:0000313|Proteomes:UP000204391};
RX PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA Rodriguez-Diaz M., Swings J., De Vos P.;
RT "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov. and
RT Virgibacillus picturae sp. nov., three novel species isolated from
RT deteriorated mural paintings, transfer of the species of the genus
RT salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov. and
RT Virgibacillus salexigens comb. nov., and emended description of the genus
RT Virgibacillus.";
RL Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000256|ARBA:ARBA00037921}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP022437; ASN07262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221MI30; -.
DR KEGG; vne:CFK40_01995; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000204391; Chromosome.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:InterPro.
DR CDD; cd07119; ALDH_BADH-GbsA; 1.
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 NCBIfam; TIGR01804; BADH; 1.
DR PANTHER; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43860:SF2; BETAINE ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000204391}.
FT DOMAIN 7..472
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 485 AA; 52954 MW; 134B627CDBFA2CFC CRC64;
MYINGEWVNA KSGETRDIIN PYNQDVIACA AEGNEEDSRA AIQAARVAFD EGSFSTLPAS
ERGEFVYRIG TLIRRDLQEL AELETLDTGK TVEESRADMA DIANVFLYFG GLADKNGGEV
IESPIPNSES KVVREPVGVC GQITPWNYPL LQAAWKIAPA LAAGNTIVMK PSEITPLTTV
KVFKLIEEAG IPKGVANLVL GSGASVGAEL SVNDDVDLIS FTGGIETGKK VMQAASHNVK
KIALELGGKN PNIVFADADF ETAVDQALNA VFFHAGQVCS AGSRLLIEES IHDEFVEVLI
ERTKQIKLGN GFDENTQSGP MISAEHRAKV ENYVEIGQKE GAKLAVGGKR PDDPELQNGF
FYLPTIFTNC TNDMRIVQEE VFGPVLTVET FQTKEEAVKL ANDTIYGLAG AVWTQDLNKA
EFVAARLRMG TVWINDFHPY FAQAPWGGYK QSGIGRELGP EGIDEYTEVK HIYRNTQPKP
VNWFK
//
