ID   ROCA_GEOSW              Reviewed;         515 AA.
AC   C5D4J5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=1-pyrroline-5-carboxylate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
DE            Short=P5C dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
DE            EC=1.2.1.88 {ECO:0000255|HAMAP-Rule:MF_00733};
DE   AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
GN   Name=rocA {ECO:0000255|HAMAP-Rule:MF_00733}; OrderedLocusNames=GWCH70_0274;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
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., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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:0000255|HAMAP-Rule:MF_00733};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00733}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00733}.
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DR   EMBL; CP001638; ACS23203.1; -; Genomic_DNA.
DR   RefSeq; WP_012749020.1; NC_012793.1.
DR   AlphaFoldDB; C5D4J5; -.
DR   SMR; C5D4J5; -.
DR   STRING; 471223.GWCH70_0274; -.
DR   EnsemblBacteria; ACS23203; ACS23203; GWCH70_0274.
DR   KEGG; gwc:GWCH70_0274; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OMA; NWNKQLT; -.
DR   OrthoDB; 744602at2; -.
DR   UniPathway; UPA00261; UER00374.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR   CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_00733; 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   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01237; D1pyr5carbox2; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..515
FT                   /note="1-pyrroline-5-carboxylate dehydrogenase"
FT                   /id="PRO_1000212739"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
SQ   SEQUENCE   515 AA;  56609 MW;  FD89044FCF9A23A5 CRC64;
     MVQPYKHEPL TDFTVEANRK AFEEALKKVE AELGKDYPLI IGGERVTTDE KIVSINPANK
     TEVIGRVSKA NKELAEKAMK VADEAFKWWS KTKPEARADI LFRAAAIVRR RKHEFSALMV
     KEAGKPWKEA DADTAEAIDF MEYYARQMLK LKDGVPVESR PGETNRFFYI PLGVGVVISP
     WNFPFAIMAG TTVASLVTGN TVLLKPASAT PVVAYKFAEV LEEAGLPAGV LNYIPGSGAE
     VGDYLVDHPR TRFISFTGSR DVGIRIYERA AKVHPGQIWL KRVIAEMGGK DGIVVDKEAD
     LELAAQSIVA SAFGFSGQKC SACSRAIIVE DVYDQVLNRV VELTKQLKVG DPADQSTFMG
     PVIDQSAYNK IMEYIEIGKK EGRLMTGGEG DDSKGFFIQP TVFADVDPNA RIMQEEIFGP
     VVAFTKAKDF DHALEIANNT EYGLTGAVIS RNRANLEKAR EEFHVGNLYF NRGCTGAIVG
     YQPFGGFNMS GTDSKAGGPD YLILHMQAKT VSEMF