UniProtKB - P09546 (PUTA_ECOLI)
Protein
Bifunctional protein PutA
Gene
putA
Organism
Escherichia coli (strain K12)
Status
Functioni
Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon.
Catalytic activityi
Cofactori
: L-proline degradation into L-glutamate Pathwayi
This protein is involved in step 1 and 2 of the subpathway that synthesizes L-glutamate from L-proline.Proteins known to be involved in the 2 steps of the subpathway in this organism are:
- Bifunctional protein PutA (putA), Bifunctional protein PutA (putA)
- Bifunctional protein PutA (putA), Bifunctional protein PutA (putA)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 883 | By similarity | 1 | |
Active sitei | 917 | By similarity | 1 |
GO - Molecular functioni
- 1-pyrroline-5-carboxylate dehydrogenase activity Source: EcoCyc
- bacterial-type cis-regulatory region sequence-specific DNA binding Source: EcoCyc
- DNA binding Source: EcoCyc
- DNA-binding transcription repressor activity Source: EcoCyc
- flavin adenine dinucleotide binding Source: EcoCyc
- identical protein binding Source: IntAct
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: InterPro
- proline dehydrogenase activity Source: UniProtKB
- sequence-specific DNA binding Source: UniProtKB
GO - Biological processi
- negative regulation of transcription, DNA-templated Source: EcoCyc
- proline biosynthetic process Source: InterPro
- proline catabolic process to glutamate Source: EcoCyc
- response to oxidative stress Source: EcoCyc
Keywordsi
Molecular function | DNA-binding, Multifunctional enzyme, Oxidoreductase, Repressor |
Biological process | Proline metabolism, Transcription, Transcription regulation |
Ligand | FAD, Flavoprotein, NAD |
Enzyme and pathway databases
BioCyci | EcoCyc:PUTA-MONOMER MetaCyc:PUTA-MONOMER |
BRENDAi | 1.2.1.88, 2026 1.5.5.2, 2026 |
UniPathwayi | UPA00261;UER00373 UPA00261;UER00374 |
Protein family/group databases
MoonProti | P09546 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:putA Synonyms:poaA Ordered Locus Names:b1014, JW0999 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: EcoCyc
Plasma Membrane
- cytoplasmic side of plasma membrane Source: EcoCyc
- plasma membrane Source: EcoCyc
Pathology & Biotechi
Chemistry databases
DrugBanki | DB03051, (S)-2-Tetrahydrofuroic acid DB03147, Flavin adenine dinucleotide DB04398, Lactic acid |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000056524 | 1 – 1320 | Bifunctional protein PutAAdd BLAST | 1320 |
Proteomic databases
jPOSTi | P09546 |
PaxDbi | P09546 |
PRIDEi | P09546 |
Expressioni
Inductioni
By proline, autorepression and catabolite repression, and is potentially nitrogen controlled.
Interactioni
Subunit structurei
Homodimer.
1 PublicationBinary interactionsi
P09546
With | #Exp. | IntAct |
---|---|---|
itself | 5 | EBI-369718,EBI-369718 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4262846, 27 interactors 849974, 1 interactor |
DIPi | DIP-10620N |
IntActi | P09546, 24 interactors |
MINTi | P09546 |
STRINGi | 511145.b1014 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P09546 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09546 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 228 – 574 | Proline dehydrogenaseAdd BLAST | 347 | |
Regioni | 653 – 1119 | Aldehyde dehydrogenaseAdd BLAST | 467 |
Sequence similaritiesi
In the N-terminal section; belongs to the proline dehydrogenase family.Curated
In the C-terminal section; belongs to the aldehyde dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | COG0506, Bacteria COG3905, Bacteria COG4230, Bacteria |
HOGENOMi | CLU_005682_1_0_6 |
InParanoidi | P09546 |
PhylomeDBi | P09546 |
Family and domain databases
DisProti | DP02030 |
Gene3Di | 1.10.1220.10, 1 hit 1.20.5.550, 1 hit 3.40.309.10, 1 hit 3.40.605.10, 1 hit |
InterProi | View protein in InterPro IPR016161, Ald_DH/histidinol_DH IPR016163, Ald_DH_C IPR016160, Ald_DH_CS_CYS IPR029510, Ald_DH_CS_GLU IPR016162, Ald_DH_N IPR015590, Aldehyde_DH_dom IPR013321, Arc_rbn_hlx_hlx IPR025703, Bifunct_PutA IPR005933, Delta1-pyrroline-5-COlate_DH-3 IPR029041, FAD-linked_oxidoreductase-like IPR041349, PRODH IPR024090, PRODH_PutA_dom_I IPR024089, PRODH_PutA_dom_I/II IPR024082, PRODH_PutA_dom_II IPR002872, Proline_DH_dom IPR010985, Ribbon_hlx_hlx |
Pfami | View protein in Pfam PF00171, Aldedh, 1 hit PF01619, Pro_dh, 1 hit PF14850, Pro_dh-DNA_bdg, 1 hit PF18327, PRODH, 1 hit |
PIRSFi | PIRSF000197, Bifunct_PutA, 1 hit |
SUPFAMi | SSF47598, SSF47598, 1 hit SSF51730, SSF51730, 1 hit SSF53720, SSF53720, 1 hit SSF81935, SSF81935, 1 hit |
TIGRFAMsi | TIGR01238, D1pyr5carbox3, 1 hit |
PROSITEi | View protein in PROSITE PS00070, ALDEHYDE_DEHYDR_CYS, 1 hit PS00687, ALDEHYDE_DEHYDR_GLU, 1 hit |
i Sequence
Sequence statusi: Complete.
P09546-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGTTTMGVKL DDATRERIKS AATRIDRTPH WLIKQAIFSY LEQLENSDTL
60 70 80 90 100
PELPALLSGA ANESDEAPTP AEEPHQPFLD FAEQILPQSV SRAAITAAYR
110 120 130 140 150
RPETEAVSML LEQARLPQPV AEQAHKLAYQ LADKLRNQKN ASGRAGMVQG
160 170 180 190 200
LLQEFSLSSQ EGVALMCLAE ALLRIPDKAT RDALIRDKIS NGNWQSHIGR
210 220 230 240 250
SPSLFVNAAT WGLLFTGKLV STHNEASLSR SLNRIIGKSG EPLIRKGVDM
260 270 280 290 300
AMRLMGEQFV TGETIAEALA NARKLEEKGF RYSYDMLGEA ALTAADAQAY
310 320 330 340 350
MVSYQQAIHA IGKASNGRGI YEGPGISIKL SALHPRYSRA QYDRVMEELY
360 370 380 390 400
PRLKSLTLLA RQYDIGINID AEESDRLEIS LDLLEKLCFE PELAGWNGIG
410 420 430 440 450
FVIQAYQKRC PLVIDYLIDL ATRSRRRLMI RLVKGAYWDS EIKRAQMDGL
460 470 480 490 500
EGYPVYTRKV YTDVSYLACA KKLLAVPNLI YPQFATHNAH TLAAIYQLAG
510 520 530 540 550
QNYYPGQYEF QCLHGMGEPL YEQVTGKVAD GKLNRPCRIY APVGTHETLL
560 570 580 590 600
AYLVRRLLEN GANTSFVNRI ADTSLPLDEL VADPVTAVEK LAQQEGQTGL
610 620 630 640 650
PHPKIPLPRD LYGHGRDNSA GLDLANEHRL ASLSSALLNS ALQKWQALPM
660 670 680 690 700
LEQPVAAGEM SPVINPAEPK DIVGYVREAT PREVEQALES AVNNAPIWFA
710 720 730 740 750
TPPAERAAIL HRAAVLMESQ MQQLIGILVR EAGKTFSNAI AEVREAVDFL
760 770 780 790 800
HYYAGQVRDD FANETHRPLG PVVCISPWNF PLAIFTGQIA AALAAGNSVL
810 820 830 840 850
AKPAEQTPLI AAQGIAILLE AGVPPGVVQL LPGRGETVGA QLTGDDRVRG
860 870 880 890 900
VMFTGSTEVA TLLQRNIASR LDAQGRPIPL IAETGGMNAM IVDSSALTEQ
910 920 930 940 950
VVVDVLASAF DSAGQRCSAL RVLCLQDEIA DHTLKMLRGA MAECRMGNPG
960 970 980 990 1000
RLTTDIGPVI DSEAKANIER HIQTMRSKGR PVFQAVRENS EDAREWQSGT
1010 1020 1030 1040 1050
FVAPTLIELD DFAELQKEVF GPVLHVVRYN RNQLPELIEQ INASGYGLTL
1060 1070 1080 1090 1100
GVHTRIDETI AQVTGSAHVG NLYVNRNMVG AVVGVQPFGG EGLSGTGPKA
1110 1120 1130 1140 1150
GGPLYLYRLL ANRPESALAV TLARQDAKYP VDAQLKAALT QPLNALREWA
1160 1170 1180 1190 1200
ANRPELQALC TQYGELAQAG TQRLLPGPTG ERNTWTLLPR ERVLCIADDE
1210 1220 1230 1240 1250
QDALTQLAAV LAVGSQVLWP DDALHRQLVK ALPSAVSERI QLAKAENITA
1260 1270 1280 1290 1300
QPFDAVIFHG DSDQLRALCE AVAARDGTIV SVQGFARGES NILLERLYIE
1310 1320
RSLSVNTAAA GGNASLMTIG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 531 | G → A in AAB59985 (PubMed:7966312).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U05212 Genomic DNA Translation: AAB59985.1 U00096 Genomic DNA Translation: AAC74099.1 AP009048 Genomic DNA Translation: BAA35791.1 X05653 Genomic DNA Translation: CAA29141.1 Sequence problems. |
PIRi | D64843 |
RefSeqi | NP_415534.1, NC_000913.3 WP_001326840.1, NZ_SSZK01000002.1 |
Genome annotation databases
EnsemblBacteriai | AAC74099; AAC74099; b1014 BAA35791; BAA35791; BAA35791 |
GeneIDi | 57731805 945600 |
KEGGi | ecj:JW0999 eco:b1014 |
PATRICi | fig|1411691.4.peg.1257 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U05212 Genomic DNA Translation: AAB59985.1 U00096 Genomic DNA Translation: AAC74099.1 AP009048 Genomic DNA Translation: BAA35791.1 X05653 Genomic DNA Translation: CAA29141.1 Sequence problems. |
PIRi | D64843 |
RefSeqi | NP_415534.1, NC_000913.3 WP_001326840.1, NZ_SSZK01000002.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1TIW | X-ray | 2.00 | A | 86-669 | [»] | |
1TJ0 | X-ray | 2.10 | A | 86-669 | [»] | |
1TJ1 | X-ray | 2.00 | A | 86-669 | [»] | |
1TJ2 | X-ray | 2.05 | A | 86-669 | [»] | |
2AY0 | X-ray | 2.10 | A/B/C/D/E/F | 1-52 | [»] | |
2FZM | X-ray | 2.30 | A | 86-669 | [»] | |
2FZN | X-ray | 2.00 | A | 86-669 | [»] | |
2GPE | X-ray | 1.90 | A/B/C/D | 1-52 | [»] | |
2RBF | X-ray | 2.25 | A/B | 1-52 | [»] | |
3E2Q | X-ray | 1.75 | A | 86-630 | [»] | |
3E2R | X-ray | 1.85 | A | 86-630 | [»] | |
3E2S | X-ray | 2.00 | A | 86-630 | [»] | |
3ITG | X-ray | 2.15 | A/B | 86-669 | [»] | |
4JNY | X-ray | 1.90 | A | 86-669 | [»] | |
4JNZ | X-ray | 1.85 | A | 86-669 | [»] | |
4O8A | X-ray | 2.00 | A | 1-669 | [»] | |
SMRi | P09546 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262846, 27 interactors 849974, 1 interactor |
DIPi | DIP-10620N |
IntActi | P09546, 24 interactors |
MINTi | P09546 |
STRINGi | 511145.b1014 |
Chemistry databases
DrugBanki | DB03051, (S)-2-Tetrahydrofuroic acid DB03147, Flavin adenine dinucleotide DB04398, Lactic acid |
Protein family/group databases
MoonProti | P09546 |
Proteomic databases
jPOSTi | P09546 |
PaxDbi | P09546 |
PRIDEi | P09546 |
Genome annotation databases
EnsemblBacteriai | AAC74099; AAC74099; b1014 BAA35791; BAA35791; BAA35791 |
GeneIDi | 57731805 945600 |
KEGGi | ecj:JW0999 eco:b1014 |
PATRICi | fig|1411691.4.peg.1257 |
Organism-specific databases
EchoBASEi | EB0794 |
Phylogenomic databases
eggNOGi | COG0506, Bacteria COG3905, Bacteria COG4230, Bacteria |
HOGENOMi | CLU_005682_1_0_6 |
InParanoidi | P09546 |
PhylomeDBi | P09546 |
Enzyme and pathway databases
UniPathwayi | UPA00261;UER00373 UPA00261;UER00374 |
BioCyci | EcoCyc:PUTA-MONOMER MetaCyc:PUTA-MONOMER |
BRENDAi | 1.2.1.88, 2026 1.5.5.2, 2026 |
Miscellaneous databases
EvolutionaryTracei | P09546 |
PROi | PR:P09546 |
Family and domain databases
DisProti | DP02030 |
Gene3Di | 1.10.1220.10, 1 hit 1.20.5.550, 1 hit 3.40.309.10, 1 hit 3.40.605.10, 1 hit |
InterProi | View protein in InterPro IPR016161, Ald_DH/histidinol_DH IPR016163, Ald_DH_C IPR016160, Ald_DH_CS_CYS IPR029510, Ald_DH_CS_GLU IPR016162, Ald_DH_N IPR015590, Aldehyde_DH_dom IPR013321, Arc_rbn_hlx_hlx IPR025703, Bifunct_PutA IPR005933, Delta1-pyrroline-5-COlate_DH-3 IPR029041, FAD-linked_oxidoreductase-like IPR041349, PRODH IPR024090, PRODH_PutA_dom_I IPR024089, PRODH_PutA_dom_I/II IPR024082, PRODH_PutA_dom_II IPR002872, Proline_DH_dom IPR010985, Ribbon_hlx_hlx |
Pfami | View protein in Pfam PF00171, Aldedh, 1 hit PF01619, Pro_dh, 1 hit PF14850, Pro_dh-DNA_bdg, 1 hit PF18327, PRODH, 1 hit |
PIRSFi | PIRSF000197, Bifunct_PutA, 1 hit |
SUPFAMi | SSF47598, SSF47598, 1 hit SSF51730, SSF51730, 1 hit SSF53720, SSF53720, 1 hit SSF81935, SSF81935, 1 hit |
TIGRFAMsi | TIGR01238, D1pyr5carbox3, 1 hit |
PROSITEi | View protein in PROSITE PS00070, ALDEHYDE_DEHYDR_CYS, 1 hit PS00687, ALDEHYDE_DEHYDR_GLU, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PUTA_ECOLI | |
Accessioni | P09546Primary (citable) accession number: P09546 Secondary accession number(s): P78296 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | November 1, 1997 | |
Last modified: | April 7, 2021 | |
This is version 203 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families