ID   ROCA_STAAR              Reviewed;         514 AA.
AC   Q6GDP4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 115.
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=SAR2634;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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   -!- FUNCTION: Oxidizes L-glutamate 5-semialdehyde (the open-chain tautomer
CC       of 1-pyrroline-5-carboxylate/P5C) to L-glutamate in the second step of
CC       proline degradation. {ECO:0000250|UniProtKB:Q2FV67}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + NAD(+) + H2O = L-glutamate + NADH
CC         + 2 H(+); Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58066; EC=1.2.1.88; Evidence={ECO:0000255|HAMAP-
CC         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; BX571856; CAG41613.1; -; Genomic_DNA.
DR   RefSeq; WP_000259692.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDP4; -.
DR   SMR; Q6GDP4; -.
DR   KEGG; sar:SAR2634; -.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   UniPathway; UPA00261; UER00374.
DR   AbasyAtlas; Q6GDP4; -.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0003842; F:L-glutamate gamma-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-ARBA.
DR   CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR   FunFam; 3.40.309.10:FF:000005; 1-pyrroline-5-carboxylate dehydrogenase 1; 1.
DR   FunFam; 3.40.605.10:FF:000045; 1-pyrroline-5-carboxylate dehydrogenase 1; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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; IPR050485; Proline_metab_enzyme.
DR   InterPro; IPR005932; RocA.
DR   InterPro; IPR047597; RocA_bacillales.
DR   NCBIfam; TIGR01237; D1pyr5carbox2; 1.
DR   NCBIfam; NF002852; PRK03137.1; 1.
DR   PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Proline metabolism.
FT   CHAIN           1..514
FT                   /note="1-pyrroline-5-carboxylate dehydrogenase"
FT                   /id="PRO_0000056517"
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;  56868 MW;  117DF65C22339CDB CRC64;
     MVVEFKNEPG YDFSVQENVD MFKKALKDVE KELGQDIPLV INGEKIFKDD KIKSINPADT
     SQVIANASKA TKQDVEDAFK AANEAYKSWK TWSANDRAEL MLRVSAIIRR RKAEIAAIMV
     YEAGKPWDEA VGDAAEGIDF IEYYARSMMD LAQGKPVLDR EGEHNKYFYK SIGTGVTIPP
     WNFPFAIMAG TTLAPVVAGN TVLLKPAEDT PYIAYKLMEI 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
//