PUTA_SALTY
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 03-AUG-2022, entry version 163.
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; OrderedLocusNames=STM1124;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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 bifunctional
RT 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 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., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX 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: molecular
RT characterization of the put operon, and DNA sequence of the put control
RT region.";
RL Mol. Gen. Genet. 213:125-133(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=LT2;
RX PubMed=1987118; DOI=10.1128/jb.173.1.211-219.1991;
RA Ostrovsky de Spicer P., O'Brien K., Maloy S.;
RT "Regulation of proline utilization in Salmonella typhimurium: a membrane-
RT 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 of the
CC put operon.
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 -!- INDUCTION: By proline, autorepression and catabolite repression, and is
CC potentially nitrogen controlled.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL20055.1; Type=Frameshift; Evidence={ECO:0000305};
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; X70843; CAA50193.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20055.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X12569; CAA31081.1; ALT_SEQ; Genomic_DNA.
DR PIR; S66279; S66279.
DR RefSeq; NP_447555.1; NC_003197.2.
DR RefSeq; WP_000537528.1; NC_003197.2.
DR AlphaFoldDB; P10503; -.
DR SMR; P10503; -.
DR STRING; 99287.STM1124; -.
DR MoonProt; P10503; -.
DR PRIDE; P10503; -.
DR EnsemblBacteria; AAL20055; AAL20055; STM1124.
DR GeneID; 2673752; -.
DR KEGG; stm:STM1124; -.
DR HOGENOM; CLU_005682_1_0_6; -.
DR OMA; PPWNFPV; -.
DR PhylomeDB; P10503; -.
DR BioCyc; MetaCyc:STM1124-MON; -.
DR BioCyc; SENT99287:STM1124-MON; -.
DR UniPathway; UPA00261; UER00373.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IMP:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:UniProtKB.
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:1901973; F:proline binding; IMP:UniProtKB.
DR GO; GO:0004657; F:proline dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051699; F:proline oxidase activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0071235; P:cellular response to proline; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR GO; GO:0006562; P:proline catabolic process; IDA:UniProtKB.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IDA:UniProtKB.
DR GO; GO:0010238; P:response to proline; IDA:UniProtKB.
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; IPR029510; Ald_DH_CS_GLU.
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 InterPro; IPR010985; Ribbon_hlx_hlx.
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; SSF47598; SSF47598; 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.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; FAD; Flavoprotein; Multifunctional enzyme; NAD;
KW Oxidoreductase; Proline metabolism; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1320
FT /note="Bifunctional protein PutA"
FT /id="PRO_0000056528"
FT REGION 228..574
FT /note="Proline dehydrogenase"
FT REGION 653..1119
FT /note="Aldehyde dehydrogenase"
FT ACT_SITE 883
FT /evidence="ECO:0000250"
FT ACT_SITE 917
FT /evidence="ECO:0000250"
FT CONFLICT 850
FT /note="G -> R (in Ref. 1; CAA50193)"
FT /evidence="ECO:0000305"
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
