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   16-JUN-2009, entry version 29.
DE   RecName: Full=1-pyrroline-5-carboxylate dehydrogenase;
DE            Short=P5C dehydrogenase;
DE            EC=1.5.1.12;
GN   Name=rocA; OrderedLocusNames=SAR2634;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2
CC       H(2)O = L-glutamate + NAD(P)H.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BX571856; CAG41613.1; -; Genomic_DNA.
DR   RefSeq; YP_041979.1; -.
DR   GeneID; 2858920; -.
DR   GenomeReviews; BX571856_GR; SAR2634.
DR   KEGG; sar:SAR2634; -.
DR   HOGENOM; Q6GDP4; -.
DR   OMA; Q6GDP4; SINPANT.
DR   BioCyc; SAUR282458:SAR2634-MON; -.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase act...; IEA:HAMAP.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00733; -; 1.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR005932; d-1-pyrroline-5-COlate_DH-2.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 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   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    514       1-pyrroline-5-carboxylate dehydrogenase.
FT                                /FTId=PRO_0000056517.
FT   ACT_SITE    286    286       By similarity.
FT   ACT_SITE    320    320       By similarity.
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
//