ID   PUTA_RHIME              Reviewed;        1224 AA.
AC   P95629;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Bifunctional protein putA;
DE   Includes:
DE     RecName: Full=Proline dehydrogenase;
DE              EC=1.5.99.8;
DE     AltName: Full=Proline oxidase;
DE   Includes:
DE     RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase;
DE              Short=P5C dehydrogenase;
DE              EC=1.5.1.12;
GN   Name=putA;
OS   Rhizobium meliloti (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GR4;
RX   MEDLINE=97157944; PubMed=9004223;
RX   DOI=10.1046/j.1365-2958.1997.1861555.x;
RA   Jimenez-Zurdo J.I., Garcia-Rodriguez F.M., Toro N.;
RT   "The Rhizobium meliloti putA gene: its role in the establishment of
RT   the symbiotic interaction with alfalfa.";
RL   Mol. Microbiol. 23:85-93(1997).
RN   [2]
RP   AUTOREGULATORY ROLE.
RX   MEDLINE=20179809; PubMed=10715000;
RX   DOI=10.1128/JB.182.7.1935-1941.2000;
RA   Soto M.J., Jimenez-Zurdo J.I., van Dillewijn P., Toro N.;
RT   "Sinorhizobium meliloti putA gene regulation: a new model within the
RT   family rhizobiaceae.";
RL   J. Bacteriol. 182:1935-1941(2000).
CC   -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
CC       nitrogen source, and also functions as a transcriptional repressor
CC       of its own gene.
CC   -!- CATALYTIC ACTIVITY: L-proline + acceptor = (S)-1-pyrroline-5-
CC       carboxylate + reduced acceptor.
CC   -!- CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2
CC       H(2)O = L-glutamate + NAD(P)H.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the proline
CC       dehydrogenase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC       dehydrogenase family.
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DR   EMBL; Y08500; CAA69727.1; -; Genomic_DNA.
DR   PIR; T43218; T43218.
DR   HSSP; P09546; 1K87.
DR   BRENDA; 1.5.1.12; 142.
DR   BRENDA; 1.5.99.8; 142.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase act...; IEA:EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:EC.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   GO; GO:0006562; P:proline catabolic process; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR005933; d-1-pyrroline-5-COlate_DH-3.
DR   InterPro; IPR002872; Proline_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   TIGRFAMs; TIGR01238; D1pyr5carbox3; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   DNA-binding; FAD; Flavoprotein; Multifunctional enzyme; NAD;
KW   Oxidoreductase; Proline metabolism; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1224       Bifunctional protein putA.
FT                                /FTId=PRO_0000056527.
FT   REGION      164    501       Proline dehydrogenase.
FT   REGION      576   1032       Aldehyde dehydrogenase.
FT   ACT_SITE    800    800       By similarity.
FT   ACT_SITE    834    834       By similarity.
SQ   SEQUENCE   1224 AA;  131191 MW;  BEC655494FCE98D1 CRC64;
     MSPNPLQKPA IDAAPAPFAD FAPPVRPQST LRRAITAAYR RPETECLPPL VEAATQSKEI
     RDAAASTARK LIEALRGKHS GSGVEGLVQE YSLSSQEGVA LMCLAERPVR IPDTATRDAL
     IRDKIADGNW KSHLGRSRSL FVNAATWGLV VTGKLTSTVN DRTLAARVTR LISRCGEPVI
     RRGVDMAMRM MGEQFVTGET IEALKRSKEL EEKGFSYSYD MLRERPTAAD AERYYRDYES
     AIHATAKPRG RGIYEGPGIS IKLSALHPRY RQAARVMGEL LPRVKALALL AKNYDIGLNI
     DAEEADRLEL SLDLLEVLCL DGDLSGWNGM GFVVQAYGKR CPFVLDFIID LARRSGRRIM
     VRLVKGAYWD AEIKRAQLDG LADFPVFTRK IHTDVSYMPR TQAACRDRCG VPQFATHNAQ
     TLAAIYHMAG KDFHVGKYEF QCLHGMGEPL YEEVVGRGKL DRPCRIYAPV GTHETLLAYL
     VRRLLENGAN SSFVHRINDP KVSIDELIAD PVEVVRAMPV VGAKHDRIAL PAVLFGDART
     NSAGFDLSNE ETLASLTEAL RESAAMKWTA LPQFATGPAA GETRTVLNPG DHRDVVGSVT
     ETRKRTHGAP CACRRRGAGL GGRLAERAAC LDRAAELMQA RMPTLLGLII REAGKSALNA
     IAEVREAIDF LRYYAEQTRR TLGPATPLGP IVCISPWNFP LAIFTGQIAA ALVAGNPVLA
     KPAEETPLIA AEGVRILREA GIPASALQLL PGDGRVGAAL VAGRDAGVMF TGSTEVARLI
     QAQLADRLSP AGRPVPLIAE TGGQNAMIVD SSALAGQVVG DVITSAFDSA GQRCSALRVL
     CLQEDVAGPH PDDAEGRAAR HCISAAPIVF SVDVGPVITS EAKDNIEKHI ERMRGLGRKV
     EQIGLASETG VGTFVPPTII ELEKLSDLQR EVFGPVLHVI RYRRDDLDRL VDDVNATGYG
     LTFGLHTRLD ETIAHVTSRI KAGNLYINRN IIGAVVGVQP FGGRGLSGTG PKAGGPLYLG
     RLVTTAPVPP QHSSVHTDPV LLDFAKWLDG KGARAEVEAA RNAGSSSALG LDLELPGPVG
     ERNLYTLHAR GRILLVPATE SGLYHQLAAA LATGNSVAID AASGLQASLK NLPQTVGLRV
     SWSKDWAADG PFAGALVEGD AERIRAVNKA IAALPGPLLL VQAASSGEIA RNPDAYCLNW
     LVEEVSASIN TAAAGGNASL MAIG
//