ID A0A062VWF1_9MICO Unreviewed; 511 AA.
AC A0A062VWF1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Betaine-aldehyde dehydrogenase {ECO:0000313|EMBL:KDA06461.1};
DE EC=1.2.1.8 {ECO:0000313|EMBL:KDA06461.1};
GN ORFNames=DC31_08495 {ECO:0000313|EMBL:KDA06461.1};
OS Microbacterium sp. CH12i.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA06461.1, ECO:0000313|Proteomes:UP000027096};
RN [1] {ECO:0000313|EMBL:KDA06461.1, ECO:0000313|Proteomes:UP000027096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH12i {ECO:0000313|EMBL:KDA06461.1,
RC ECO:0000313|Proteomes:UP000027096};
RA Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT shallow groundwater in Cape Hallet, Antarctica.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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:KDA06461.1}.
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DR EMBL; JHET01000003; KDA06461.1; -; Genomic_DNA.
DR RefSeq; WP_051606424.1; NZ_JHET01000003.1.
DR AlphaFoldDB; A0A062VWF1; -.
DR STRING; 1479651.DC31_08495; -.
DR Proteomes; UP000027096; Unassembled WGS sequence.
DR GO; GO:0018480; F:5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity; IEA:InterPro.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:1901023; P:4-hydroxyphenylacetate catabolic process; IEA:InterPro.
DR CDD; cd07093; ALDH_F8_HMSADH; 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; IPR011985; DH_HpaE.
DR NCBIfam; TIGR02299; HpaE; 1.
DR PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43720:SF2; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 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:UP000027096}.
FT DOMAIN 23..483
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 511 AA; 55470 MW; D82C006591208D31 CRC64;
MTDSRIPANL PDHIQHYIDG EFVDSVDGDT FDVLDPVTNE NYTTAAAGKK ADIDLAVAAA
TRAFKEGPWP RMLPRERSRV LHRIADIVES RDQRLAELES FDSGLPITQA LGQARRAAEN
FRFFADLIVA QADDTFKVPG RQINYVNRKP IGVAGLITPW NTPFMLESWK LGPALATGNT
VVLKPAEFTP LSASLWAGIF EEAGLPKGVF NLVNGLGEDA GDALVKHPDV PLISFTGESS
TGQLIFANAA PFLKGLSMEL GGKSPAVVFA DADLEAAINA TIFGVFSLNG ERCTAGSRIL
VERSVYEEFV EKYAAQAKRV KVGLPNDPTT EVGALVHPEH YDKVMSYVEI GKGEARLVAG
GGRPEGFETG NYVAPTVFAD VSPDARIFQE EIFGPVVAIT PFENDEEALA LANNTRYGLA
AYIWTNDLKR AHNFAGNVEA GMVWLNSNNV RDLRTPFGGV KASGLGHEGG YRSIDFYTDQ
QAVHITLGEV HNPTFGKNEI HETDLDDPDP R
//
