ID   ROCA_STAAT              Reviewed;         514 AA.
AC   A8Z3F5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-NOV-2008, entry version 11.
DE   RecName: Full=1-pyrroline-5-carboxylate dehydrogenase;
DE            Short=P5C dehydrogenase;
DE            EC=1.5.1.12;
GN   Name=rocA; OrderedLocusNames=USA300HOU_2549;
OS   Staphylococcus aureus (strain USA300 / TCH1516).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=451516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA   Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA   Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y.,
RA   Igboeli O., Petrosino J., Tirumalai M., Uzman A., Fox G.E.,
RA   Cardenas A.M., Muzny D.M., Hemphill L., Ding Y., Dugan S., Blyth P.R.,
RA   Buhay C.J., Dinh H.H., Hawes A.C., Holder M., Kovar C.L., Lee S.L.,
RA   Liu W., Nazareth L.V., Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT   "Subtle genetic changes enhance virulence of methicillin resistant and
RT   sensitive Staphylococcus aureus.";
RL   BMC Microbiol. 7:99-99(2007).
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.
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DR   EMBL; CP000730; ABX30535.1; -; Genomic_DNA.
DR   RefSeq; YP_001576414.1; -.
DR   GeneID; 5774925; -.
DR   GenomeReviews; CP000730_GR; USA300HOU_2549.
DR   KEGG; sax:USA300HOU_2549; -.
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_DHase_CS.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR015590; Aldehyde_DHase.
DR   InterPro; IPR005932; d-1-pyrroline-5-COlate_DHase-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_1000083342.
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
//