(data stored in ACNUC7421 zone)

SWISSPROT: C3MF64_SINFN

ID   C3MF64_SINFN            Unreviewed;      1235 AA.
AC   C3MF64;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197};
DE   Includes:
DE     RecName: Full=Proline dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              EC=1.5.5.2 {ECO:0000256|PIRNR:PIRNR000197};
DE     AltName: Full=Proline oxidase {ECO:0000256|PIRNR:PIRNR000197};
DE   Includes:
DE     RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              Short=P5C dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              EC=1.2.1.88 {ECO:0000256|PIRNR:PIRNR000197};
DE     AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
GN   Name=putA1 {ECO:0000313|EMBL:ACP23901.1};
GN   OrderedLocusNames=NGR_c00980 {ECO:0000313|EMBL:ACP23901.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23901.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23901.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
CC       nitrogen source. {ECO:0000256|PIRNR:PIRNR000197}.
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         Evidence={ECO:0000256|PIRNR:PIRNR000197};
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         Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC       {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC       {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the proline
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
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DR   EMBL; CP001389; ACP23901.1; -; Genomic_DNA.
DR   RefSeq; WP_012706686.1; NC_012587.1.
DR   RefSeq; YP_002824654.1; NC_012587.1.
DR   STRING; 394.NGR_c00980; -.
DR   EnsemblBacteria; ACP23901; ACP23901; NGR_c00980.
DR   GeneID; 7790677; -.
DR   KEGG; rhi:NGR_c00980; -.
DR   PATRIC; fig|394.7.peg.2892; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG0506; LUCA.
DR   eggNOG; COG4230; LUCA.
DR   HOGENOM; HOG000253911; -.
DR   KO; K13821; -.
DR   OMA; VRIYAPV; -.
DR   OrthoDB; 14333at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
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; 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;
DR   PRODOM; C3MF64.
DR   SWISS-2DPAGE; C3MF64.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR000197};
KW   FAD {ECO:0000256|PIRNR:PIRNR000197};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000197};
KW   NAD {ECO:0000256|PIRNR:PIRNR000197};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000197,
KW   ECO:0000313|EMBL:ACP23901.1};
KW   Proline metabolism {ECO:0000256|PIRNR:PIRNR000197};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN       31     78       PRODH. {ECO:0000259|Pfam:PF18327}.
FT   DOMAIN       86    197       Pro_dh-DNA_bdg. {ECO:0000259|Pfam:
FT                                PF14850}.
FT   DOMAIN      207    504       Pro_dh. {ECO:0000259|Pfam:PF01619}.
FT   DOMAIN      588   1027       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    812    812       {ECO:0000256|PIRSR:PIRSR000197-1}.
FT   ACT_SITE    846    846       {ECO:0000256|PIRSR:PIRSR000197-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   1235 AA;  131629 MW;  214E79D9EF39206E CRC64;
     MSQTQLQKPT ISTDAAPAPF ADFAPPIRTQ TTLRQAITAA YRRPETECLP PLVEAATLPR
     GTRDAAAGTA RKLVEALRAK HKGSGVEGLV QEYSLSSQEG VALMCLAEAL LRIPDTATRD
     ALIRDKISDG NWKSHLGGGR SLFVNAATWG LVVTGKLTST VNDRSLAAAL TRLISRCGEP
     VIRRGVDMAM RMMGEQFVTG ETIDEALRRA RALEQKGFRY SYDMLGEAAT TAADAERYYK
     DYEAAIHAIG KASAGRGIYE GPGISIKLSA LHPRYARTQA ARVMGELLPK VKALALLAKT
     YDIGFNIDAE EADRLELSLD LLEELCLDSD LADWNGMGFV VQAYGKRCPF VLDFIIDLAR
     RAGRRIMVRL VKGAYWDAEI KRAQLDGLED FPVFTRKIHT DVSYIACARK LLSATDAVFP
     QFATHNAQTL ATIHHMAGKD FHVGKYEFQC LHGMGEPLYE EVVGRENLGR PCRIYAPVGT
     HETLLAYLVR RLLENGANSS FVHRIADPGV SIDALIADPV EIVRAMPVVG AKHEKIALPA
     ELFGAARPNS AGLDISNEAT LAALTETLKA SAAIGWTAAP QLATGAASGE TRPVVNPGDH
     RDRVGSVTET SEEDAKRAVR LAAEAAPSWA AVSPAERAAC LDRAADLMQA RMPTLLGLIV
     REAGKSLLNA IAEVREAIDF LRYYAEQTRR TLGQAHRPLG PVICISPWNF PLAIFTGQIA
     AALVAGNPVL AKPAEETPLI AAEGVRILHE AGVPASALQL LPGDGRVGAA LVAAPQTAGV
     MFTGSTEVAR LIQAQLADRL SPAGRPIPLI AETGGQNAMI VDSSALAEQV VGDVIASAFD
     SAGQRCSALR VLCLQEDIAD RTLAMLKGAL HELNIGRTDR LSVDVGPVIS AEAKDIIETH
     IERMRGLGRK VEQIGLAAET EAGTFVPPTI IELEKLADLQ REVFGPVLHV IRYRRDNLDR
     LIDDINATGY GLTFGLHTRL DETIAHVTSR IKAGNLYVNR NIIGAVVGVQ PFGGRGLSGT
     GPKAGGPLYL GRLVTPAPVP PQHSSVHIDP TLLDFAKWLD GKGATAEAET ARNAGSSSAL
     GLDLELPGPV GERNLYALHP RGRVLLVPAT ESGLYHQLAA ALATGNSVVV DAACGLQASL
     KSLPHSVALR VSWSKDWAAD GPFAGALVEG DAERIRQVNK AIAALPGPLV LVQAASGEEI
     ARNPDAYCLN WLVEEVSTSI NTAAAGGNAS LMTIG
//

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