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Database: UniProt
Entry: Q9RW56_DEIRA
LinkDB: Q9RW56_DEIRA
Original site: Q9RW56_DEIRA 
ID   Q9RW56_DEIRA            Unreviewed;       523 AA.
AC   Q9RW56;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE            EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN   OrderedLocusNames=DR_0813 {ECO:0000313|EMBL:AAF10392.1};
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF10392.1, ECO:0000313|Proteomes:UP000002524};
RN   [1] {ECO:0000313|EMBL:AAF10392.1, ECO:0000313|Proteomes:UP000002524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC         glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC         Evidence={ECO:0000256|ARBA:ARBA00001468};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004786}.
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DR   EMBL; AE000513; AAF10392.1; -; Genomic_DNA.
DR   PIR; C75471; C75471.
DR   RefSeq; NP_294537.1; NC_001263.1.
DR   RefSeq; WP_010887459.1; NZ_JMLF01000005.1.
DR   AlphaFoldDB; Q9RW56; -.
DR   STRING; 243230.DR_0813; -.
DR   PaxDb; 243230-DR_0813; -.
DR   EnsemblBacteria; AAF10392; AAF10392; DR_0813.
DR   GeneID; 69517057; -.
DR   KEGG; dra:DR_0813; -.
DR   PATRIC; fig|243230.17.peg.993; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_0; -.
DR   InParanoid; Q9RW56; -.
DR   OrthoDB; 9762913at2; -.
DR   BRENDA; 1.2.1.88; 1856.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR   CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR005932; RocA.
DR   NCBIfam; TIGR01237; D1pyr5carbox2; 1.
DR   PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002524}.
FT   DOMAIN          53..519
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   523 AA;  56626 MW;  C54323A499BC8B60 CRC64;
     MIKVQDYRPQ PFTDFTKEEN VQAYQAALAK VRKELLGKHY PLIIDGQEVD TEGKIQSINP
     CDTSEVVGTT AKATIGDAEN ALQGAWKAFE SWKKWDMDAR ARILLKAAAI LKRRRLEACA
     LMSIEVGKNY AEADVEVAEA IDFLEYYARS AMKYAGFGSS ETTWFEGEEN GLMSIPLGVG
     VSISPWNFPC AIFVGMAAAP IVAGNCVVVK PAEDAGLIAG FMVDILREAG LPAGVLQFLP
     GVGKEVGEYL TTHAKTRFIT FTGSRAVGLH INEVAAKVQP GQKWIKRVIM ELGGKDGLIV
     DETADIENAI TAATQGAFGF NGQKCSAMSR LIVVDSVYDE VVNGFVERAK ALKMGTGEEN
     ANVTAVVNQM SFNKIKGYLE LAPSEGKVLL GGEATGEANG KQGYYIQPTI VGDVDRNSRL
     AQEEIFGPVV AVLRAKDWQD ALDIANSTEY GLTGGVCSNS RERLEQARAE FEVGNLYFNR
     KITGAIVGVQ PFGGYNMSGT DSKAGGPDYL SNFMQLKTVT ERW
//
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