Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional protein PutA

Gene

putA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol.
L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.

Cofactori

Pathwayi: L-proline degradation into L-glutamate

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:
  1. Bifunctional protein PutA (putA)
  2. Bifunctional protein PutA (putA)
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei883By similarity1
Active sitei917By similarity1

GO - Molecular functioni

  • 1-pyrroline-5-carboxylate dehydrogenase activity Source: EcoCyc
  • aldehyde dehydrogenase (NAD) activity Source: GO_Central
  • bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding Source: EcoCyc
  • DNA binding Source: EcoCyc
  • flavin adenine dinucleotide binding Source: EcoCyc
  • proline dehydrogenase activity Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional repressor activity, bacterial-type RNA polymerase core promoter proximal region sequence-specific binding Source: EcoCyc

GO - Biological processi

  • proline biosynthetic process Source: InterPro
  • proline catabolic process to glutamate Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW

Keywords - Molecular functioni

Oxidoreductase, Repressor

Keywords - Biological processi

Proline metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciEcoCyc:PUTA-MONOMER.
ECOL316407:JW0999-MONOMER.
MetaCyc:PUTA-MONOMER.
BRENDAi1.2.1.88. 2026.
1.5.5.2. 2026.
UniPathwayiUPA00261; UER00373.
UPA00261; UER00374.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein PutA
Including the following 2 domains:
Proline dehydrogenase (EC:1.5.5.2)
Alternative name(s):
Proline oxidase
Delta-1-pyrroline-5-carboxylate dehydrogenase (EC:1.2.1.88)
Short name:
P5C dehydrogenase
Alternative name(s):
L-glutamate gamma-semialdehyde dehydrogenase
Gene namesi
Name:putA
Synonyms:poaA
Ordered Locus Names:b1014, JW0999
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10801. putA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: EcoCyc

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.
DB04398. Lactic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000565241 – 1320Bifunctional protein PutAAdd BLAST1320

Proteomic databases

EPDiP09546.
PaxDbiP09546.
PRIDEiP09546.

Expressioni

Inductioni

By proline, autorepression and catabolite repression, and is potentially nitrogen controlled.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262846. 6 interactors.
DIPiDIP-10620N.
IntActiP09546. 23 interactors.
MINTiMINT-1267731.
STRINGi511145.b1014.

Structurei

Secondary structure

11320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Helixi12 – 24Combined sources13
Helixi29 – 45Combined sources17
Helixi90 – 98Combined sources9
Helixi103 – 114Combined sources12
Helixi118 – 136Combined sources19
Turni137 – 139Combined sources3
Helixi141 – 152Combined sources12
Turni153 – 156Combined sources4
Helixi159 – 173Combined sources15
Beta strandi175 – 177Combined sources3
Helixi178 – 183Combined sources6
Helixi208 – 212Combined sources5
Helixi227 – 235Combined sources9
Helixi241 – 256Combined sources16
Helixi257 – 259Combined sources3
Beta strandi262 – 264Combined sources3
Helixi265 – 270Combined sources6
Helixi273 – 276Combined sources4
Turni277 – 279Combined sources3
Beta strandi281 – 286Combined sources6
Helixi294 – 315Combined sources22
Helixi319 – 322Combined sources4
Beta strandi325 – 328Combined sources4
Helixi330 – 333Combined sources4
Helixi337 – 339Combined sources3
Helixi342 – 363Combined sources22
Beta strandi367 – 369Combined sources3
Helixi374 – 376Combined sources3
Helixi377 – 388Combined sources12
Helixi391 – 393Combined sources3
Beta strandi399 – 404Combined sources6
Helixi410 – 423Combined sources14
Beta strandi428 – 433Combined sources6
Helixi438 – 448Combined sources11
Helixi459 – 474Combined sources16
Turni477 – 479Combined sources3
Beta strandi480 – 485Combined sources6
Helixi489 – 498Combined sources10
Helixi505 – 507Combined sources3
Beta strandi509 – 513Combined sources5
Turni514 – 516Combined sources3
Helixi518 – 521Combined sources4
Turni522 – 524Combined sources3
Helixi528 – 530Combined sources3
Beta strandi537 – 543Combined sources7
Helixi546 – 548Combined sources3
Helixi550 – 561Combined sources12
Helixi562 – 564Combined sources3
Helixi566 – 569Combined sources4
Helixi577 – 580Combined sources4
Helixi584 – 595Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TIWX-ray2.00A86-669[»]
1TJ0X-ray2.10A86-669[»]
1TJ1X-ray2.00A86-669[»]
1TJ2X-ray2.05A86-669[»]
2AY0X-ray2.10A/B/C/D/E/F1-52[»]
2FZMX-ray2.30A86-669[»]
2FZNX-ray2.00A86-669[»]
2GPEX-ray1.90A/B/C/D1-52[»]
2RBFX-ray2.25A/B1-52[»]
3E2QX-ray1.75A86-630[»]
3E2RX-ray1.85A86-630[»]
3E2SX-ray2.00A86-630[»]
3ITGX-ray2.15A/B86-669[»]
4JNYX-ray1.90A86-669[»]
4JNZX-ray1.85A86-669[»]
4O8AX-ray2.00A1-669[»]
ProteinModelPortaliP09546.
SMRiP09546.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09546.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni228 – 574Proline dehydrogenaseAdd BLAST347
Regioni653 – 1119Aldehyde dehydrogenaseAdd BLAST467

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

eggNOGiENOG4105C26. Bacteria.
COG0506. LUCA.
COG4230. LUCA.
HOGENOMiHOG000253911.
InParanoidiP09546.
KOiK13821.
OMAiYSLDTQE.
PhylomeDBiP09546.

Family and domain databases

Gene3Di1.10.2060.10. 1 hit.
1.20.5.550. 1 hit.
3.20.20.220. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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.
IPR025703. Bifunct_PutA.
IPR005933. Delta1-pyrroline-5-COlate_DH-3.
IPR029041. FAD-linked_oxidoreductase-like.
IPR024090. PRODH_PutA_dom_I.
IPR024089. PRODH_PutA_dom_I/II.
IPR024082. PRODH_PutA_dom_II.
IPR002872. Proline_DH_dom.
IPR010985. Ribbon_hlx_hlx.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
PF01619. Pro_dh. 1 hit.
PF14850. Pro_dh-DNA_bdg. 1 hit.
[Graphical view]
PIRSFiPIRSF000197. Bifunct_PutA. 1 hit.
SUPFAMiSSF47598. SSF47598. 1 hit.
SSF51730. SSF51730. 1 hit.
SSF53720. SSF53720. 1 hit.
SSF81935. SSF81935. 1 hit.
TIGRFAMsiTIGR01238. D1pyr5carbox3. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09546-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:1,320
Mass (Da):143,815
Last modified:November 1, 1997 - v3
Checksum:iE4920143D536F7F9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti531G → A in AAB59985 (PubMed:7966312).Curated1

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.
PIRiD64843.
RefSeqiNP_415534.1. NC_000913.3.
WP_001326840.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74099; AAC74099; b1014.
BAA35791; BAA35791; BAA35791.
GeneIDi945600.
KEGGiecj:JW0999.
eco:b1014.
PATRICi32117257. VBIEscCol129921_1052.

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.
PIRiD64843.
RefSeqiNP_415534.1. NC_000913.3.
WP_001326840.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TIWX-ray2.00A86-669[»]
1TJ0X-ray2.10A86-669[»]
1TJ1X-ray2.00A86-669[»]
1TJ2X-ray2.05A86-669[»]
2AY0X-ray2.10A/B/C/D/E/F1-52[»]
2FZMX-ray2.30A86-669[»]
2FZNX-ray2.00A86-669[»]
2GPEX-ray1.90A/B/C/D1-52[»]
2RBFX-ray2.25A/B1-52[»]
3E2QX-ray1.75A86-630[»]
3E2RX-ray1.85A86-630[»]
3E2SX-ray2.00A86-630[»]
3ITGX-ray2.15A/B86-669[»]
4JNYX-ray1.90A86-669[»]
4JNZX-ray1.85A86-669[»]
4O8AX-ray2.00A1-669[»]
ProteinModelPortaliP09546.
SMRiP09546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262846. 6 interactors.
DIPiDIP-10620N.
IntActiP09546. 23 interactors.
MINTiMINT-1267731.
STRINGi511145.b1014.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.
DB04398. Lactic Acid.

Proteomic databases

EPDiP09546.
PaxDbiP09546.
PRIDEiP09546.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74099; AAC74099; b1014.
BAA35791; BAA35791; BAA35791.
GeneIDi945600.
KEGGiecj:JW0999.
eco:b1014.
PATRICi32117257. VBIEscCol129921_1052.

Organism-specific databases

EchoBASEiEB0794.
EcoGeneiEG10801. putA.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG0506. LUCA.
COG4230. LUCA.
HOGENOMiHOG000253911.
InParanoidiP09546.
KOiK13821.
OMAiYSLDTQE.
PhylomeDBiP09546.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00373.
UPA00261; UER00374.
BioCyciEcoCyc:PUTA-MONOMER.
ECOL316407:JW0999-MONOMER.
MetaCyc:PUTA-MONOMER.
BRENDAi1.2.1.88. 2026.
1.5.5.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP09546.
PROiP09546.

Family and domain databases

Gene3Di1.10.2060.10. 1 hit.
1.20.5.550. 1 hit.
3.20.20.220. 1 hit.
3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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.
IPR025703. Bifunct_PutA.
IPR005933. Delta1-pyrroline-5-COlate_DH-3.
IPR029041. FAD-linked_oxidoreductase-like.
IPR024090. PRODH_PutA_dom_I.
IPR024089. PRODH_PutA_dom_I/II.
IPR024082. PRODH_PutA_dom_II.
IPR002872. Proline_DH_dom.
IPR010985. Ribbon_hlx_hlx.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
PF01619. Pro_dh. 1 hit.
PF14850. Pro_dh-DNA_bdg. 1 hit.
[Graphical view]
PIRSFiPIRSF000197. Bifunct_PutA. 1 hit.
SUPFAMiSSF47598. SSF47598. 1 hit.
SSF51730. SSF51730. 1 hit.
SSF53720. SSF53720. 1 hit.
SSF81935. SSF81935. 1 hit.
TIGRFAMsiTIGR01238. D1pyr5carbox3. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPUTA_ECOLI
AccessioniPrimary (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: November 2, 2016
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.