ID K0K5C8_SACES Unreviewed; 474 AA.
AC K0K5C8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000313|EMBL:CCH31748.1};
DE EC=1.2.1.19 {ECO:0000313|EMBL:CCH31748.1};
GN Name=prr3 {ECO:0000313|EMBL:CCH31748.1};
GN OrderedLocusNames=BN6_44670 {ECO:0000313|EMBL:CCH31748.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH31748.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH31748.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; HE804045; CCH31748.1; -; Genomic_DNA.
DR RefSeq; WP_015101860.1; NC_019673.1.
DR AlphaFoldDB; K0K5C8; -.
DR STRING; 1179773.BN6_44670; -.
DR KEGG; sesp:BN6_44670; -.
DR PATRIC; fig|1179773.3.peg.4473; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_11; -.
DR BioCyc; SESP1179773:BN6_RS21625-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd07092; ALDH_ABALDH-YdcW; 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; IPR015657; Aminobutyraldehyde_DH.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF307; GAMMA-AMINOBUTYRALDEHYDE 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:UP000006281}.
FT DOMAIN 21..470
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 474 AA; 50166 MW; 329E877F2353D3D5 CRC64;
MTDAVHNVIG GQTRETIAGA TTELVDPSTG EVCDTAPLST VEDVDAAYRA AVDAFEVWRD
TTPGQRQVAL LRCADALERR AAEFVAAECR DTGKPTATTL SDEVLAAVDA LRFFAGAARV
LPGVGATEYA PGHTSYVRRE PVGVVGQVAP WNYPLLMAMW KIAPALAAGN TVVLKPADTT
PVTAVMFGVL AAEFLPAGVL NVVCGDRDTG RAVVAHPAAA MVSITGSTRA GVEVARSAAD
RVARTHLELG GNAPVVVFAD ADLDAAVEGI VATGFFNAGQ DCTAASRVLV DRRVHDEFAA
RLAERARTVH TGPPSDPTAH YGPLNNADQF ARVRAILDGL PDHARITAGG EAVGERGYFL
APTVVTGVRQ DDAVVQQENF GPVLTVQPFT DEAHALRLAC GVEQGLAASV WTSDHGRALR
MSARLDFGCV WINTHMVLVP EMPHGGFKQS GYGKDLSQYS LEEYTRVKHV MHKL
//
