PUTA_ECOLI
ID PUTA_ECOLI Reviewed; 1320 AA.
AC P09546; P78296;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 207.
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; Synonyms=poaA; OrderedLocusNames=b1014, JW0999;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7966312; DOI=10.1006/jmbi.1994.1696;
RA Ling M., Allen S.W., Wood J.M.;
RT "Sequence analysis identifies the proline dehydrogenase and delta 1-
RT pyrroline-5-carboxylate dehydrogenase domains of the multifunctional
RT Escherichia coli PutA protein.";
RL J. Mol. Biol. 243:950-956(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RC STRAIN=K12;
RX PubMed=3325781; DOI=10.1007/bf00325707;
RA Nakao T., Yamato I., Anraku Y.;
RT "Nucleotide sequence of putC, the regulatory region for the put regulon of
RT Escherichia coli K12.";
RL Mol. Gen. Genet. 210:364-368(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-669 IN COMPLEX WITH FAD, AND
RP HOMODIMERIZATION.
RX PubMed=12514740; DOI=10.1038/nsb885;
RA Lee Y.-H., Nadaraia S., Gu D., Becker D.F., Tanner J.J.;
RT "Structure of the proline dehydrogenase domain of the multifunctional PutA
RT flavoprotein.";
RL Nat. Struct. Biol. 10:109-114(2003).
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12514740}.
CC -!- INTERACTION:
CC P09546; P09546: putA; NbExp=5; IntAct=EBI-369718, EBI-369718;
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}.
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DR EMBL; U05212; AAB59985.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74099.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35791.1; -; Genomic_DNA.
DR EMBL; X05653; CAA29141.1; ALT_SEQ; Genomic_DNA.
DR PIR; D64843; D64843.
DR RefSeq; NP_415534.1; NC_000913.3.
DR RefSeq; WP_001326840.1; NZ_SSZK01000002.1.
DR PDB; 1TIW; X-ray; 2.00 A; A=86-669.
DR PDB; 1TJ0; X-ray; 2.10 A; A=86-669.
DR PDB; 1TJ1; X-ray; 2.00 A; A=86-669.
DR PDB; 1TJ2; X-ray; 2.05 A; A=86-669.
DR PDB; 2AY0; X-ray; 2.10 A; A/B/C/D/E/F=1-52.
DR PDB; 2FZM; X-ray; 2.30 A; A=86-669.
DR PDB; 2FZN; X-ray; 2.00 A; A=86-669.
DR PDB; 2GPE; X-ray; 1.90 A; A/B/C/D=1-52.
DR PDB; 2RBF; X-ray; 2.25 A; A/B=1-52.
DR PDB; 3E2Q; X-ray; 1.75 A; A=86-630.
DR PDB; 3E2R; X-ray; 1.85 A; A=86-630.
DR PDB; 3E2S; X-ray; 2.00 A; A=86-630.
DR PDB; 3ITG; X-ray; 2.15 A; A/B=86-669.
DR PDB; 4JNY; X-ray; 1.90 A; A=86-669.
DR PDB; 4JNZ; X-ray; 1.85 A; A=86-669.
DR PDB; 4O8A; X-ray; 2.00 A; A=1-669.
DR PDBsum; 1TIW; -.
DR PDBsum; 1TJ0; -.
DR PDBsum; 1TJ1; -.
DR PDBsum; 1TJ2; -.
DR PDBsum; 2AY0; -.
DR PDBsum; 2FZM; -.
DR PDBsum; 2FZN; -.
DR PDBsum; 2GPE; -.
DR PDBsum; 2RBF; -.
DR PDBsum; 3E2Q; -.
DR PDBsum; 3E2R; -.
DR PDBsum; 3E2S; -.
DR PDBsum; 3ITG; -.
DR PDBsum; 4JNY; -.
DR PDBsum; 4JNZ; -.
DR PDBsum; 4O8A; -.
DR AlphaFoldDB; P09546; -.
DR SMR; P09546; -.
DR BioGRID; 4262846; 27.
DR BioGRID; 849974; 1.
DR DIP; DIP-10620N; -.
DR IntAct; P09546; 24.
DR MINT; P09546; -.
DR STRING; 511145.b1014; -.
DR DrugBank; DB03051; (S)-2-Tetrahydrofuroic acid.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB04398; Lactic acid.
DR MoonProt; P09546; -.
DR jPOST; P09546; -.
DR PaxDb; P09546; -.
DR PRIDE; P09546; -.
DR EnsemblBacteria; AAC74099; AAC74099; b1014.
DR EnsemblBacteria; BAA35791; BAA35791; BAA35791.
DR GeneID; 945600; -.
DR KEGG; ecj:JW0999; -.
DR KEGG; eco:b1014; -.
DR PATRIC; fig|1411691.4.peg.1257; -.
DR EchoBASE; EB0794; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG3905; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR HOGENOM; CLU_005682_1_0_6; -.
DR InParanoid; P09546; -.
DR OMA; PPWNFPV; -.
DR PhylomeDB; P09546; -.
DR BioCyc; EcoCyc:PUTA-MON; -.
DR BioCyc; MetaCyc:PUTA-MON; -.
DR BRENDA; 1.2.1.88; 2026.
DR BRENDA; 1.5.5.2; 2026.
DR UniPathway; UPA00261; UER00373.
DR UniPathway; UPA00261; UER00374.
DR EvolutionaryTrace; P09546; -.
DR PRO; PR:P09546; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR DisProt; DP02030; -.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000056524"
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 531
FT /note="G -> A (in Ref. 1; AAB59985)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2GPE"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:2GPE"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:2GPE"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:3E2Q"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:3E2Q"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1TIW"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:4JNZ"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:4JNZ"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3E2Q"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 294..315
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 342..363
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 410..423
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 459..474
FT /evidence="ECO:0007829|PDB:3E2Q"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 489..498
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:3E2Q"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:3E2Q"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:3E2Q"
FT STRAND 537..543
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 550..561
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:3ITG"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:3E2Q"
FT HELIX 584..595
FT /evidence="ECO:0007829|PDB:3E2Q"
SQ SEQUENCE 1320 AA; 143815 MW; E4920143D536F7F9 CRC64;
MGTTTMGVKL DDATRERIKS AATRIDRTPH WLIKQAIFSY LEQLENSDTL PELPALLSGA
ANESDEAPTP AEEPHQPFLD FAEQILPQSV SRAAITAAYR RPETEAVSML LEQARLPQPV
AEQAHKLAYQ LADKLRNQKN ASGRAGMVQG LLQEFSLSSQ EGVALMCLAE ALLRIPDKAT
RDALIRDKIS NGNWQSHIGR SPSLFVNAAT WGLLFTGKLV STHNEASLSR SLNRIIGKSG
EPLIRKGVDM AMRLMGEQFV TGETIAEALA NARKLEEKGF RYSYDMLGEA ALTAADAQAY
MVSYQQAIHA IGKASNGRGI YEGPGISIKL SALHPRYSRA QYDRVMEELY PRLKSLTLLA
RQYDIGINID AEESDRLEIS LDLLEKLCFE PELAGWNGIG FVIQAYQKRC PLVIDYLIDL
ATRSRRRLMI RLVKGAYWDS EIKRAQMDGL EGYPVYTRKV YTDVSYLACA KKLLAVPNLI
YPQFATHNAH TLAAIYQLAG QNYYPGQYEF QCLHGMGEPL YEQVTGKVAD GKLNRPCRIY
APVGTHETLL AYLVRRLLEN GANTSFVNRI ADTSLPLDEL VADPVTAVEK LAQQEGQTGL
PHPKIPLPRD LYGHGRDNSA GLDLANEHRL ASLSSALLNS ALQKWQALPM LEQPVAAGEM
SPVINPAEPK DIVGYVREAT PREVEQALES AVNNAPIWFA TPPAERAAIL HRAAVLMESQ
MQQLIGILVR EAGKTFSNAI AEVREAVDFL HYYAGQVRDD FANETHRPLG PVVCISPWNF
PLAIFTGQIA AALAAGNSVL AKPAEQTPLI AAQGIAILLE AGVPPGVVQL LPGRGETVGA
QLTGDDRVRG VMFTGSTEVA TLLQRNIASR LDAQGRPIPL IAETGGMNAM IVDSSALTEQ
VVVDVLASAF DSAGQRCSAL RVLCLQDEIA DHTLKMLRGA MAECRMGNPG RLTTDIGPVI
DSEAKANIER HIQTMRSKGR PVFQAVRENS EDAREWQSGT FVAPTLIELD DFAELQKEVF
GPVLHVVRYN RNQLPELIEQ INASGYGLTL GVHTRIDETI AQVTGSAHVG NLYVNRNMVG
AVVGVQPFGG EGLSGTGPKA GGPLYLYRLL ANRPESALAV TLARQDAKYP VDAQLKAALT
QPLNALREWA ANRPELQALC TQYGELAQAG TQRLLPGPTG ERNTWTLLPR ERVLCIADDE
QDALTQLAAV LAVGSQVLWP DDALHRQLVK ALPSAVSERI QLAKAENITA QPFDAVIFHG
DSDQLRALCE AVAARDGTIV SVQGFARGES NILLERLYIE RSLSVNTAAA GGNASLMTIG
