ID L0IUW8_9MYCO Unreviewed; 515 AA.
AC L0IUW8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Putative succinate-semialdehyde dehydrogenase [NADP(+)] 2 {ECO:0000256|ARBA:ARBA00039663};
DE EC=1.2.1.79 {ECO:0000256|ARBA:ARBA00039122};
GN ORFNames=Mycsm_01415 {ECO:0000313|EMBL:AGB21827.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB21827.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.79;
CC Evidence={ECO:0000256|ARBA:ARBA00036722};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP003078; AGB21827.1; -; Genomic_DNA.
DR RefSeq; WP_015305410.1; NC_019966.1.
DR AlphaFoldDB; L0IUW8; -.
DR STRING; 212767.Mycsm_01415; -.
DR KEGG; msa:Mycsm_01415; -.
DR PATRIC; fig|710686.3.peg.1425; -.
DR HOGENOM; CLU_005391_5_1_11; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000010844; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd07099; ALDH_DDALDH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 11..465
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 515 AA; 55424 MW; 304C3F8E65E34133 CRC64;
MTAIQPDTRR STIEVRNPAD GTVVGVVPND SADTVAAKAR ELRLFQPEWE ALGPRGRKTW
LLKFQDWVLD NAEHLTDVVQ SETGKVRADA SIEAPMTAGL LDYWARNAEA FLGDRHPRPH
NLLMMTKRLT TAYRPYPVVG LIIPWNFPFA NAALDGIAAL AAGAALLLKP SEVTPLSAVE
FARGWTEIGA PPVLALTTGY AETGAAVIAN SDYVHFTGST ATGRKVAVAC AERLIPYSLE
LGGKDPAVVL ADADLERAAN GIAWGGMTNS GQVCVSIERV YVEAPIYDEF VAKLTDKVSS
LRQGQDDDKY RFDVGAMATA AQRDIVARHV DEAVAGGARV TTGGKPTGVG TFFQPTVLAD
VDQSMSCMRE ETFGPTLPVV KVADEEEAIR LANDSRYGLS ATVWTSDPAR AERVARKIEA
GAVNINDAMA NGFQFAVPMP GWKDSGIGAR NGGAEGILKY CRAQAITTPR IPAQANEPLW
YPYSRRKFRF GLGLMRATAA RGVRRLGLKP RGGAR
//
