ID   ROCA_BACC1              Reviewed;         515 AA.
AC   P62028;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=BCE_0338;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017194; AAS39274.1; -; Genomic_DNA.
DR   RefSeq; WP_000259559.1; NC_003909.8.
DR   AlphaFoldDB; P62028; -.
DR   SMR; P62028; -.
DR   EnsemblBacteria; AAS39274; AAS39274; BCE_0338.
DR   GeneID; 59159242; -.
DR   KEGG; bca:BCE_0338; -.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OMA; NWNKQLT; -.
DR   UniPathway; UPA00261; UER00374.
DR   Proteomes; UP000002527; 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_0000056504"
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;  56198 MW;  36199CA65B718606 CRC64;
     MVVAYKHEPF TDFSVEANKL AFEEGLKKVE SYLGQDYPLI IGGEKITTED KIVSVNPANK
     EELVGRVSKA SRELAEKAMQ VADETFQTWR KSKPEMRADI LFRAAAIVRR RKHEFSAILV
     KEAGKPWNEA DADTAEAIDF MEYYGRQMLK LKDGIPVESR PIEYNRFSYI PLGVGVIISP
     WNFPFAIMAG MTTAALVSGN TVLLKPASTT PVVAAKFMEV LEEAGLPAGV VNFVPGSGSE
     VGDYLVDHPR TRFISFTGSR DVGIRIYERA AKVNPGQIWL KRVIAEMGGK DTIVVDKEAD
     LELAAKSIVA SAFGFSGQKC SACSRAVIHE DVYDHVLNRA VELTKELTVA NPAVLGTNMG
     PVNDQAAFDK VMSYVAIGKE EGRILAGGEG DDSKGWFIQP TIVADVAEDA RLMKEEIFGP
     VVAFCKAKDF DHALAIANNT EYGLTGAVIS NNRDHIEKAR EDFHVGNLYF NRGCTGAIVG
     YQPFGGFNMS GTDSKAGGPD YLALHMQAKT TSETL