ID   B4UF03_ANASK            Unreviewed;       543 AA.
AC   B4UF03;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00032259};
DE            EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
DE   AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00032259};
GN   OrderedLocusNames=AnaeK_0877 {ECO:0000313|EMBL:ACG72113.1};
OS   Anaeromyxobacter sp. (strain K).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=447217 {ECO:0000313|EMBL:ACG72113.1, ECO:0000313|Proteomes:UP000001871};
RN   [1] {ECO:0000313|EMBL:ACG72113.1, ECO:0000313|Proteomes:UP000001871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|EMBL:ACG72113.1,
RC   ECO:0000313|Proteomes:UP000001871};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA   Beliaev A.;
RT   "Complete sequence of Anaeromyxobacter sp. K.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP001131; ACG72113.1; -; Genomic_DNA.
DR   RefSeq; WP_012524940.1; NC_011145.1.
DR   AlphaFoldDB; B4UF03; -.
DR   KEGG; ank:AnaeK_0877; -.
DR   HOGENOM; CLU_005391_4_1_7; -.
DR   OrthoDB; 9762913at2; -.
DR   UniPathway; UPA00261; UER00374.
DR   Proteomes; UP000001871; Chromosome.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR   CDD; cd07123; ALDH_F4-17_P5CDH; 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; IPR005931; P5CDH/ALDH4A1.
DR   NCBIfam; TIGR01236; D1pyr5carbox1; 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.
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   Proline metabolism {ECO:0000256|ARBA:ARBA00023062}.
FT   DOMAIN          58..521
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   543 AA;  59337 MW;  D942FE298AB6EEF2 CRC64;
     MSNGAFRIPD PRNEPVLSYA PGTPERAALK ARLAELSSRE LEIPLVIGGR EVRTGRIAEV
     RVPHRHGQRL ARFHQAGPAE VQAAIEAALE ARKTWSAMPP HERAAVLLKA ADLLAGPWRQ
     TLNAATMLGQ SKTPYQAEID SACEIIDFWR WNPHFMERMH HDQPVSPPGQ WNRTEYRALE
     GFVFAVTPFN FTSIAANLPT APALMGNTVV WKPASSAIYS AWHVMKVLEA AGLPPGVINF
     VPGPGRAVGD PALGSADLAG LHFTGSTGVF QQMWRTIGEN LPRYHGYPRI VGETGGKDFV
     FVHPSADVDA AATALVRGAF EYQGQKCSAA SRAYVPESLW PQLRERLLGM VAEIKMGEVE
     DFTTFMGAVI DRGAFDSIRK HIGVARASSQ AKILAGGGCD DSKGFFVEPT VIETVNPHFK
     LMEEEIFGPV LTVYVYADIR LDEALELCST TSPYGLTGAI FARDRDAVAD LTRRLADTAG
     NFYVNDKPTG AVVGQQPFGG ARASGTNDKA GSIANLYRWV SIRSIKETFD PAVRFEYPYM
     REK
//