ID   PUTA_SALTY              Reviewed;        1320 AA.
AC   P10503;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 4.
DT   16-JUN-2009, entry version 83.
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; OrderedLocusNames=STM1124;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93241961; PubMed=8479928; DOI=10.1093/nar/21.7.1676;
RA   Allen S.W., Senti-Willis A.E., Maloy S.R.;
RT   "DNA sequence of the putA gene from Salmonella typhimurium: a
RT   bifunctional membrane-associated dehydrogenase that binds DNA.";
RL   Nucleic Acids Res. 21:1676-1676(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Maloy S.R.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX   MEDLINE=89127131; PubMed=2851701; DOI=10.1007/BF00333408;
RA   Hahn D.R., Myers R.S., Kent C.R., Maloy S.R.;
RT   "Regulation of proline utilization in Salmonella typhimurium:
RT   molecular characterization of the put operon, and DNA sequence of the
RT   put control region.";
RL   Mol. Gen. Genet. 213:125-133(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC   STRAIN=LT2;
RX   MEDLINE=91100285; PubMed=1987118;
RA   Ostrovsky de Spicer P., O'Brien K., Maloy S.;
RT   "Regulation of proline utilization in Salmonella typhimurium: a
RT   membrane-associated dehydrogenase binds DNA in vitro.";
RL   J. Bacteriol. 173:211-219(1991).
CC   -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
CC       nitrogen source and also function as a transcriptional repressor
CC       of the put operon.
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   -!- INDUCTION: By proline, autorepression and catabolite repression,
CC       and is potentially nitrogen controlled.
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL20055.1; Type=Frameshift; Positions=1048;
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; X70843; CAA50193.1; -; Genomic_DNA.
DR   EMBL; AE008748; AAL20055.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X12569; CAA31081.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S66279; S66279.
DR   HSSP; P09546; 1K87.
DR   SMR; P10503; 2-49, 87-612.
DR   PhosSite; P10503; -.
DR   GenomeReviews; AE006468_GR; STM1124.
DR   KEGG; stm:STM1124; -.
DR   HOGENOM; P10503; -.
DR   BioCyc; STYP99287:STM1124-MON; -.
DR   BRENDA; 1.5.1.12; 2.
DR   BRENDA; 1.5.99.8; 2.
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.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; DNA-binding; FAD; Flavoprotein;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Proline metabolism;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1   1320       Bifunctional protein putA.
FT                                /FTId=PRO_0000056528.
FT   REGION      228    574       Proline dehydrogenase.
FT   REGION      653   1119       Aldehyde dehydrogenase.
FT   ACT_SITE    883    883       By similarity.
FT   ACT_SITE    917    917       By similarity.
FT   CONFLICT    850    850       G -> R (in Ref. 1; CAA50193).
SQ   SEQUENCE   1320 AA;  144090 MW;  6F38C93EE6A5FD4D CRC64;
     MGTTTMGVKL DDATRERIKM AASRIDRTPH WLIKQAIFSY LDKLENSDTL PELPALFVGA
     ANESEEPVAP QDEPHQPFLE FAEQILPQSV SRAAITAAWR RPETDAVSML MEQARLSPPV
     AEQAHKLAYQ LAEKLRNQKS ASGRAGMVQG LLQEFSLSSQ EGVALMCLAE ALLRIPDKAT
     RDALIRDKIS NGNWQSHIGR SPSLFVNAAT WGLLFTGRLV STHNEANLSR SLNRIIGKSG
     EPLIRKGVDM AMRLMGEQFV TGETIAQALA NARKLEEKGF RYSYDMLGEA ALTAADAQAY
     MVSYQQAIHA IGKASNGRGI YEGPGISIKL SALHPRYSRA QYDRVMEELY PRLKSLTLLA
     RQYDIGLNID AEEADRLEIS LDLLEKLCFE PELAGWNGIG FVIQAYQKRC PLVIDYLVDL
     ASRSRRRLMI RLVKGAYWDS EIKRAQMEGL EGYPVYTRKV YTDVSYLACA KKLLAVPNLI
     YPQFATHNAH TLAAIYHLAG QNYYPGQYEF QCLHGMGEPL YEQVTGKVAD GKLNRPCRIY
     APVGTHETLL AYLVRRLLEN GANTSFVNRI ADATLPLDEL VADPVEAVEK LAQQEGQAGI
     PHPKIPLPRD LYGEGRINSA GLDLANEHRL ASLSSALLSN AMQKWQAKPV LEQPVADGEM
     TPVINPAEPK DIVGWGREAT ESEVEQALQN AVNQAPVWFA TPPQERAAIL QRAAVLMEDQ
     MQQLIGLLVR EAGKTFSNAI AEVREAVDFL HYYAGQVRDD FDNETHRPLG PVVCISPWNF
     PLAIFTGQIA AALAAGNSVL AKPAEQTSLI AAQGIAILLE AGVPPGVVQL LPGRGETVGA
     QLTADARVRG VMFTGSTEVA TLLQRNIATR LDAQGRPIPL IAETGGMNAM IVDSSALTEQ
     VVVDVLASAF DSAGQRCSAL RVLCLQDDIA EHTLKMLRGA MAECRMGNPG RLTTDIGPVI
     DSEAKANIER HIQTMRAKGR PVFQAARENS DDAQEWQTGT FVMPTLIELE NFAELEKEVF
     GPVLHVVRYN RNQLAELIEQ INASGYGLTL GVHTRIDETI AQVTGSAHVG NLYVNRNMVG
     AVVGVQPFGG EGLSGTGPKA GGPLYLYRLL AHRPPNALNT TLTRQDARYP VDAQLKTTLL
     APLTALTQWA ADRPALQTLC RQFADLAQAG TQRLLPGPTG ERNTWTLLPR ERVLCLADDE
     QDALTQLAAV LAVGSQALWS DDAFHRDLAK RLPAAVAARV QFAKAETLMA QPFDAVIFHG
     DSDKLRTVCE AVAAREGAIV SVQGFARGES NILLERLYIE RSLSVNTAAA GGNASLMTIG
//