ID   ROCA_BACMK              Reviewed;         515 AA.
AC   A9VRG6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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};
GN   OrderedLocusNames=BcerKBAB4_0290;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
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; CP000903; ABY41556.1; -; Genomic_DNA.
DR   RefSeq; WP_012260230.1; NC_010184.1.
DR   AlphaFoldDB; A9VRG6; -.
DR   SMR; A9VRG6; -.
DR   STRING; 315730.BcerKBAB4_0290; -.
DR   EnsemblBacteria; ABY41556; ABY41556; BcerKBAB4_0290.
DR   KEGG; bwe:BcerKBAB4_0290; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OMA; NWNKQLT; -.
DR   UniPathway; UPA00261; UER00374.
DR   Proteomes; UP000002154; 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_1000189848"
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;  56232 MW;  1DE9B2027E7522EE CRC64;
     MVVAYKHEPF TDFSVEANKL AFEEGLKKVE SYLGQDYPLI IGGEKITTED KIVSVNPANK
     EELVGRVSKA SRELAEKAMQ VADATFQTWR KSKPEMRADI LFRAAAIVRR RKHEFSAILV
     KEAGKPWNEA DADTAEAIDF MEYYARQMLK LKDGMPVESR PIEYNRFSYI PLGVGVIISP
     WNFPFAIMAG MTTAAVVSGN TVLLKPASTT PVVAAKFMEV LEEAGLPAGV VNFVPGNGSE
     VGDYLVDHPR TRFVSFTGSR DVGIRIYERA AKVNPGQIWL KRVIAEMGGK DTIVVDKEAD
     LELAAKSIVA SAFGFSGQKC SACSRAVIHE DVYDHVLNRA VELTKELTVG NPDAKDINMG
     PVNDQAAFDK VMSYVAIGKE EGKIVSGGEG DDSKGWFIQP TIVADVAEDA RLMKEEIFGP
     VVAFCKAKDF DHALAIANNT EYGLTGAVLS NNRDHIEKAR EDFHVGNLYF NRGCTGAIVG
     YQPFGGFNMS GTDSKAGGPD YLALHMQAKT TSETL