ID ROCA_STAES Reviewed; 514 AA. AC Q8CN04; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 42. DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase; DE Short=P5C dehydrogenase; DE EC=1.5.1.12; GN Name=rocA; OrderedLocusNames=SE_2116; OS Staphylococcus epidermidis (strain ATCC 12228). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22832016; PubMed=12950922; RX DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). 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; AE015929; AAO05758.1; -; Genomic_DNA. DR RefSeq; NP_765671.1; -. DR HSSP; Q28399; 1O9J. DR GeneID; 1057207; -. DR GenomeReviews; AE015929_GR; SE_2116. DR KEGG; sep:SE2116; -. DR HOGENOM; Q8CN04; -. DR OMA; Q8CN04; SINPANT. DR BioCyc; SEPI176280:SE_2116-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_0000056520. FT ACT_SITE 286 286 By similarity. FT ACT_SITE 320 320 By similarity. SQ SEQUENCE 514 AA; 56876 MW; 99EE786D43629FF4 CRC64; MVVPFKNEPG IDFSVQTNVE RFNEELRKVK AQLGQDIPLV INGEKLTKTD TFNSVNPANT SQLIAKVSKA TQDDIEKAFE SANHAYQSWK KWSHKDRAEL LLRVAAIIRR RKEEISAIMV YEAGKPWDEA VGDAAEGIDF IEYYARSMME LADGKPVLDR EGEHNRYFYK PIGTGVTIPP WNFPFAIMAG TTLAPVVAGN TVLLKPAEDT VLTAYKLMEI LEEAGLPQGV VNFVPGDPKE IGDYLVDHKD THFVTFTGSR ATGTRIYERS AVVQEGQQFL KRVIAEMGGK DAIVVDNNVD TDLAAEAIVT SAFGFSGQKC SACSRAIVHQ DVHDEILEKA IQLTQKLTLG NTEENTFMGP VINQKQFDKI KNYIEIGKKE GKLETGGGTD DSTGYFIEPT IFSGLQSADR IMQEEIFGPV VGFIKVKDFD EAIEVANDTD YGLTGAVITN HREHWIKAVN EFDVGNLYLN RGCTAAVVGY HPFGGFKMSG TDAKTGSPDY LLNFLEQKVV SEMF //