ID   ROCA_BACCN              Reviewed;         515 AA.
AC   A7GKJ4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=Bcer98_0289;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS20652.1; -; Genomic_DNA.
DR   RefSeq; WP_011983411.1; NC_009674.1.
DR   AlphaFoldDB; A7GKJ4; -.
DR   SMR; A7GKJ4; -.
DR   STRING; 315749.Bcer98_0289; -.
DR   PRIDE; A7GKJ4; -.
DR   EnsemblBacteria; ABS20652; ABS20652; Bcer98_0289.
DR   GeneID; 56415846; -.
DR   KEGG; bcy:Bcer98_0289; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OMA; NWNKQLT; -.
DR   OrthoDB; 744602at2; -.
DR   UniPathway; UPA00261; UER00374.
DR   Proteomes; UP000002300; Chromosome.
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; IPR029510; Ald_DH_CS_GLU.
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.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..515
FT                   /note="1-pyrroline-5-carboxylate dehydrogenase"
FT                   /id="PRO_1000083339"
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;  56146 MW;  F9A75ECE9538EF06 CRC64;
     MVVAYKHEPF TDFSVEANKL AFEEGLKKVE SYLGQDYPLI IGGEKITTED KIVSVNPANK
     EEVIGSVSKA SRELAEKAMQ VADETFQTWR KSKPEMRADI LFRAAAIVRR RKHEFSAILV
     KEAGKPWNEA DADTAEAIDF MEYYGRQMLK LKDGIPVESR PIEYNRFSYI PLGVGVIISP
     WNFPFAIMAG MTTAALVSGN TVLLKPASTT PVVAAKFMEV LEEAGLPAGV VNFIPGSGSE
     VGDYLVDHPR TRFISFTGSR DVGIRIYERA AKVHPGQIWL KRVIAEMGGK DTIVVDKEAD
     LELAAKSIVA SAFGFSGQKC SACSRAVIHE EVYDQVLNRA VELTKELTVG NPAEKGTNMG
     PVNDQAAFDK VMSYVAIGKE EGKIVAGGEG DDSKGWFIQP TIVADVAEDA RLMKEEIFGP
     VVAFCKAKDF DHALAIANNT EYGLTGAVIS NNRAHIEKAR EDFHVGNLYF NRGCTGAIVG
     YQPFGGFNMS GTDSKAGGPD YLALHMQAKT TSEML