ID   ROCA_STAAS              Reviewed;         514 AA.
AC   Q6G6C0;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, 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=SAS2440;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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}.
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DR   EMBL; BX571857; CAG44256.1; -; Genomic_DNA.
DR   RefSeq; WP_000259686.1; NC_002953.3.
DR   AlphaFoldDB; Q6G6C0; -.
DR   SMR; Q6G6C0; -.
DR   KEGG; sas:SAS2440; -.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OMA; NWNKQLT; -.
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; 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..514
FT                   /note="1-pyrroline-5-carboxylate dehydrogenase"
FT                   /id="PRO_0000056518"
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   514 AA;  56808 MW;  BA2229760A2DBBCB CRC64;
     MVVEFKNEPG YDFSVQENVD MFKKALKDVE KELGQDIPLV INGEKIFKDD KIKSINPADT
     SQVIANASKA TKQDVEDAFK AANEAYKSWK TWSANDRAEL MLRVSAIIRR RKAEIAAIMV
     YEAGKPWDEA VGDAAEGIDF IEYYARSMMD LAQGKPVLDR EGEHNKYFYK SIGTGVTIPP
     WNFPFAIMAG TTLAPVVAGN IVLLKPAEDT PYIAYKLMGI LEEAGLPKGV VNFVPGDPKE
     IGDYLVDHKD THFVTFTGSR ATGTRIYERS AVVQEGQNFL KRVIAEMGGK DAIVVDENID
     TDMAAEAIVT SAFGFSGQKC SACSRAIVHK DVYDEVLEKS IKLTKELTLG NTVDNTYMGP
     VINKKQFDKI KNYIEIGKEE GKLEQGGGTD DSKGYFVEPT IISGLKSKDR IMQEEIFGPV
     VGFVKVNDFD EAIEVANDTD YGLTGAVITN NREHWIKAVN EFDVGNLYLN RGCTSAVVGY
     HPFGGFKMSG TDAKTGSPDY LLHFLEQKVV SEMF