PUTA_RHIML
ID PUTA_RHIML Reviewed; 1224 AA.
AC P95629;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Bifunctional protein PutA;
DE Includes:
DE RecName: Full=Proline dehydrogenase;
DE EC=1.5.5.2;
DE AltName: Full=Proline oxidase;
DE Includes:
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase;
DE Short=P5C dehydrogenase;
DE EC=1.2.1.88;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
GN Name=putA;
OS Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=382;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GR4;
RX PubMed=9004223; 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 the
RT symbiotic interaction with alfalfa.";
RL Mol. Microbiol. 23:85-93(1997).
RN [2]
RP AUTOREGULATORY ROLE.
RX PubMed=10715000; 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 family
RT 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 of
CC its own gene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:132124; EC=1.5.5.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
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. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; Y08500; CAA69727.1; -; Genomic_DNA.
DR PIR; T43218; T43218.
DR AlphaFoldDB; P95629; -.
DR SMR; P95629; -.
DR STRING; 382.DU99_02490; -.
DR PRIDE; P95629; -.
DR UniPathway; UPA00261; UER00373.
DR UniPathway; UPA00261; UER00374.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.5.550; -; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR025703; Bifunct_PutA.
DR InterPro; IPR005933; Delta1-pyrroline-5-COlate_DH-3.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR041349; PRODH.
DR InterPro; IPR024090; PRODH_PutA_dom_I.
DR InterPro; IPR024089; PRODH_PutA_dom_I/II.
DR InterPro; IPR024082; PRODH_PutA_dom_II.
DR InterPro; IPR002872; Proline_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR Pfam; PF14850; Pro_dh-DNA_bdg; 1.
DR Pfam; PF18327; PRODH; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR SUPFAM; SSF81935; SSF81935; 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
FT /note="Bifunctional protein PutA"
FT /id="PRO_0000056527"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..501
FT /note="Proline dehydrogenase"
FT REGION 576..1032
FT /note="Aldehyde dehydrogenase"
FT ACT_SITE 800
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 834
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
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
