ID G6A1Q5_9PROT Unreviewed; 476 AA.
AC G6A1Q5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=NAD-dependent aldehyde dehydrogenase {ECO:0000313|EMBL:EHI48640.1};
DE EC=1.2.1.19 {ECO:0000313|EMBL:EHI48640.1};
GN ORFNames=HIMB100_00022250 {ECO:0000313|EMBL:EHI48640.1};
OS SAR116 cluster alpha proteobacterium HIMB100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI48640.1, ECO:0000313|Proteomes:UP000004261};
RN [1] {ECO:0000313|EMBL:EHI48640.1, ECO:0000313|Proteomes:UP000004261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX PubMed=22675578; DOI=10.4056/sigs.1854551;
RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA Kyrpides N.C., Rappe M.S.;
RT "Draft genome sequence of strain HIMB100, a cultured representative of the
RT SAR116 clade of marine Alphaproteobacteria.";
RL Stand. Genomic Sci. 5:269-278(2011).
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:EHI48640.1}.
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DR EMBL; AFXB01000010; EHI48640.1; -; Genomic_DNA.
DR AlphaFoldDB; G6A1Q5; -.
DR STRING; 909943.HIMB100_00022250; -.
DR PATRIC; fig|909943.3.peg.2295; -.
DR eggNOG; COG1012; Bacteria.
DR OrthoDB; 9802947at2; -.
DR Proteomes; UP000004261; Unassembled WGS sequence.
DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000004261}.
FT DOMAIN 20..471
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 476 AA; 50522 MW; 2A62ECA4C43D3806 CRC64;
MNITMSIING QQLASHLPVF EKRYPATGEV IAKVQPATTD MLDQAVRHAQ AAQQDWAKMA
AHERARILGR IAGALHQHNE QLSALEVQDV GKVYAEALSA DVPSGAEAFE FFASLCATYH
GTSHKWPDAI GYTQRVPLGV CAGIGAWNYP VQVACWKAAP ALAAGNAFIL KPSEETPLTA
NALAEIFQQA GLPDGLFQVI HGDHEIGQAI CAHKGIAKVS LTGGVDTGRL IMAQSAATLK
KVTLELGGKA PLLIFADGDF DLAVQTALDA NFYTAGEVCS NATRVFVEDS IADAFTQAVT
ARAADLQIGD PMNPQTQIGA LISEPHMRSV LQHIERAKQE GASVLTGGEQ VRPMGCADGY
FVSPTILGNC TDDMACVKDE IFGPVMSVLT FADEQEAITR ANDTAFGLGA GIITSDLSRA
HRVADQLQAG NVWINSYNLI PPGLPFGGSK QSGFGREGSV YALEAYTEVK ATYVQL
//
