ID   ROCA_STAS1              Reviewed;         514 AA.
AC   Q4A0E7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-NOV-2008, entry version 26.
DE   RecName: Full=1-pyrroline-5-carboxylate dehydrogenase;
DE            Short=P5C dehydrogenase;
DE            EC=1.5.1.12;
GN   Name=rocA; OrderedLocusNames=SSP0311;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE17456.1; -; Genomic_DNA.
DR   RefSeq; YP_300401.1; -.
DR   GeneID; 3615883; -.
DR   GenomeReviews; AP008934_GR; SSP0311.
DR   KEGG; ssp:SSP0311; -.
DR   NMPDR; fig|342451.4.peg.108; -.
DR   HOGENOM; Q4A0E7; -.
DR   BioCyc; SSAP342451:SSP0311-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_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_0000056523.
FT   ACT_SITE    286    286       By similarity.
FT   ACT_SITE    320    320       By similarity.
SQ   SEQUENCE   514 AA;  56749 MW;  095E5E6121CEA548 CRC64;
     MVVNYHNEPS IDFTDSKNVE SFKEALKKVK GELNQKIPLV INGEEKFTKD TYQSINPANT
     TEVIAEVSKA TQKDVDDAFE AANEAYKSWK RWSHKDRAEF LIRVAAIIRR RKEEISAVMV
     YEAGKPWDEA VGDAAEGIDF IEYYARSMME LADGKPVLDR EGEHNKYFYK PIGTGVTIPP
     WNFPFAIMAG TTLAPVVAGN TVLLKPAEDT PLTAYKLMEI LEEAGLPKGV VNFVPGDPKE
     IGDYLVDSVH THFVTFTGSR ATGTRIFERA AKVQDGQQFL KRVIAEMGGK DAIVVDKDID
     TDLAAESIVS SAFGFSGQKC SACSRAIVHK DVYDEVLEKA VALTKNLTVG NTENNTYMGP
     VINQKQFDKI KNYIEIGSKE GKLKQGGGTD DATGYFVEPT IIANLKSSDQ IMQEEIFGPV
     VGFVKGKDFE ELLEIANDTD YGLTGAVITN NRENWIEAVE SYDVGNLYLN RGCTSAVVGY
     HPFGGFKMSG TDAKTGSPDY LLNFLEQKVV SEMF
//