(data stored in ACNUC7421 zone)

SWISSPROT: Q4ZZ46_PSEU2

ID   Q4ZZ46_PSEU2            Unreviewed;      1300 AA.
AC   Q4ZZ46;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 93.
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   OrderedLocusNames=Psyr_0506 {ECO:0000313|EMBL:AAY35576.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35576.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35576.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35576.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000075; AAY35576.1; -; Genomic_DNA.
DR   RefSeq; YP_233614.2; NC_007005.1.
DR   STRING; 205918.Psyr_0506; -.
DR   EnsemblBacteria; AAY35576; AAY35576; Psyr_0506.
DR   GeneID; 3365982; -.
DR   KEGG; psb:Psyr_0506; -.
DR   PATRIC; fig|205918.7.peg.525; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG0506; LUCA.
DR   eggNOG; COG4230; LUCA.
DR   HOGENOM; HOG000253911; -.
DR   KO; K13821; -.
DR   OMA; VRIYAPV; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000000426; 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; 1.10.1220.10; -; 1.
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; IPR013321; Arc_rbn_hlx_hlx.
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;
DR   PRODOM; Q4ZZ46.
DR   SWISS-2DPAGE; Q4ZZ46.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR000197,
KW   ECO:0000256|SAAS:SAAS00993492}; 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:AAY35576.1};
KW   Proline metabolism {ECO:0000256|PIRNR:PIRNR000197};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN       70    117       PRODH. {ECO:0000259|Pfam:PF18327}.
FT   DOMAIN      129    240       Pro_dh-DNA_bdg. {ECO:0000259|Pfam:
FT                                PF14850}.
FT   DOMAIN      251    550       Pro_dh. {ECO:0000259|Pfam:PF01619}.
FT   DOMAIN      642   1087       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    864    864       {ECO:0000256|PIRSR:PIRSR000197-1}.
FT   ACT_SITE    898    898       {ECO:0000256|PIRSR:PIRSR000197-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   1300 AA;  140911 MW;  FB2009AC66900B9D CRC64;
     MKAAAHSIDR TPHWLIKQAI FNYLEKLESG ATLLELDGAA GKDNEDRGEL AEEAGLQCFL
     DFAESIQPQS VLRAAITSAY RRPEPEVVPM LLEQARLSAP VAEATNKMAA SIAEKLRNQK
     SAGGRAGIVQ GLLQEFSLSS QEGVALMCLA EALLRIPDKG TRDALIRDKI SNGNWQPHLG
     NSPSLFVNAA TWGLLLTGRL VATHNEAGLT SSLSRIIGKS GEPMIRKGVD MAMRLMGEQF
     VTGETIGEAL ANASRFEAKG FRYSYDMLGE AALTEHDAQK YLASYEQAIH SIGKASHGRG
     IYEGPGISIK LSALHPRYSR AQYERVMDEL YPRLLSLTLL AKQYDIGLNI DAEEADRLEL
     SLDLLERLCF EPQLTGWNGI GFVIQAYQKR CPYVIDYVID LARRSRHRLM IRLVKGAYWD
     SEIKRAQVEG LEGYPVYTRK VYTDVSYIAC ARKLLAAPEV IYPQFATHNA HTLAAIYQIA
     GQNYYPGQYE FQCLHGMGEP LYEQVVGKVA DGKLNRPCRV YAPVGTHETL LAYLVRRLLE
     NGANTSFVNR IADHSISIQE LVADPVSQIE RMATQEGGFG LPHPRIPLPR DLYGTERANS
     SGIDMANEHR LASLSSALLA TAHNDWKAAP MLGCPASAGT LSAALNPSDL RDVVGHVQEA
     SLQDVDNAIQ CALSAGPIWQ ATPPVERAAI LERAADLMEA EIQPLMGLLV REAGKTFANA
     IAEVREAVDF LRYYAVQARN DFTNDGHRPL GPVVCISPWN FPLAIFSGQV AAALAAGNPV
     LAKPAEQTPL IAAQAVRLLL EAGIPEGVVQ LLPGRGETVG AGLVGDERVK GVMFTGSTEV
     ARLLQRNVAG RLDSQGRPIP LIAETGGQNA MIVDSSALTE QVVIDVVSSA FDSAGQRCSA
     LRVLCLQEDS ADRVIEMLKG AMAENRLGNP ERLSVDIGPV IDAEAKAGIE KHIQAMRDKG
     RTVYQVAIAD SAELKRGTYV MPTLIELESF DELQREIFGP VLHVVRYKRK ELGLLIDQIN
     ASGYGLTLGV HTRIDETIAK VIDNVNAGNV YVNRNIVGAV VGVQPFGGEG LSGTGPKAGG
     PLYLYRLLST RPQDAIEKSF VRSDALSAPD TRLREVLGKP LQALKAWAAS NQQSDLDALC
     SQYAEQSQSG ITRQLAGPTG ERNSYAILPR EHVLCLADDE NDLLIQLAAV LAVGSSAVWP
     ETDIGKPLRA RLPKDVQARI KLIPDWAKDE VIFDAVLHHG DSDQLRAICQ QIAQRSGAIV
     GVNGLSHGET NVPLERLVIE RALSVNTAAA GGNASLMTIG
//

If you have problems or comments...

PBIL Back to PBIL home page