ID A6T7A5_KLEP7 Unreviewed; 1326 AA.
AC A6T7A5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197};
DE Includes:
DE RecName: Full=Proline dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE EC=1.5.5.2 {ECO:0000256|PIRNR:PIRNR000197};
DE AltName: Full=Proline oxidase {ECO:0000256|PIRNR:PIRNR000197};
DE Includes:
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE Short=P5C dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE EC=1.2.1.88 {ECO:0000256|PIRNR:PIRNR000197};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
GN Name=putA {ECO:0000313|EMBL:ABR76476.1};
GN ORFNames=KPN_01041 {ECO:0000313|EMBL:ABR76476.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR76476.1, ECO:0000313|Proteomes:UP000000265};
RN [1] {ECO:0000313|EMBL:ABR76476.1, ECO:0000313|Proteomes:UP000000265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
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 [2] {ECO:0000313|EMBL:ABR76476.1, ECO:0000313|Proteomes:UP000000265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
CC nitrogen source. {ECO:0000256|PIRNR:PIRNR000197}.
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 Evidence={ECO:0000256|ARBA:ARBA00001468,
CC ECO:0000256|PIRNR:PIRNR000197};
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 Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2.
CC {ECO:0000256|PIRNR:PIRNR000197}.
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786, ECO:0000256|PIRNR:PIRNR000197}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the proline
CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
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DR EMBL; CP000647; ABR76476.1; -; Genomic_DNA.
DR STRING; 272620.KPN_01041; -.
DR jPOST; A6T7A5; -.
DR PaxDb; 272620-KPN_01041; -.
DR EnsemblBacteria; ABR76476; ABR76476; KPN_01041.
DR KEGG; kpn:KPN_01041; -.
DR HOGENOM; CLU_005682_1_1_6; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000000265; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProt.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR CDD; cd07125; ALDH_PutA-P5CDH; 1.
DR CDD; cd22233; RHH_CopAso-like; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR Gene3D; 1.10.1220.10; Met repressor-like; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 1.
DR Gene3D; 1.20.5.550; Single Helix bin; 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; 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; IPR005933; PutA_C.
DR InterPro; IPR048798; PutA_RHH.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR NCBIfam; TIGR01238; D1pyr5carbox3; 1.
DR PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
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 Pfam; PF21775; PutA_1st; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR SUPFAM; SSF81935; N-terminal domain of bifunctional PutA protein; 1.
DR SUPFAM; SSF47598; Ribbon-helix-helix; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PIRNR:PIRNR000197};
KW FAD {ECO:0000256|PIRNR:PIRNR000197};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000197};
KW NAD {ECO:0000256|PIRNR:PIRNR000197};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000197};
KW Proline metabolism {ECO:0000256|PIRNR:PIRNR000197};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 17..49
FT /note="PutA RHH"
FT /evidence="ECO:0000259|Pfam:PF21775"
FT DOMAIN 95..142
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 153..265
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 274..575
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 665..1111
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 889
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 923
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1326 AA; 145151 MW; 07FDFE68A77F4C89 CRC64;
MTGVLSMGTT TMGVKLDDAT RERIKSAASR IDRTPHWLIK QAIFNYLEKL ENDETLPELP
ALLSGAANES DDASEPTEEP YQPFLEFAEQ ILPQSVSRAA ITAAWRRPET DAVPMLLEQA
RLPQPLGEQA HKLAYQLAEK LRNQKTASGR AGMVQSLLQE FSLSSQEGVA LMCLAEALLR
IPDKATRDAL IRDKISNGNW QSHIGRSPSL FVNAATWGLL FTGKLVSTHN ETSLSRSLNR
IIGKSGEPLI RKGVDMAMRL MGEQFVTGET IAEALANARK LEEKGFRYSY DMLGEAALTA
ADAQAYMVSY QQAIHAIGKA SNGRGIYEGP GISIKLSALH PRYSRAQYDR VMEELYPRLK
SLTLLARQYD IGINIDAEEA DRLEISLDLL EKLCFEPELA GWNGIGFVIQ AYQKRCPFVI
DYLIDLATRS RRRLMIRLVK GAYWDSEIKR AQMEGLEGYP VYTRKVYTDV SYLACAKKLL
AVPNLIYPQF ATHNAHTLAA IYQLAGQNYY PGQYEFQCLH GMGEPLYEQV VGKVADGKLN
RPCRIYAPVG THETLLAYLV RRLLENGANT SFVNRIADNT LPLDELVADP VSAVEKLAQQ
EGQAGLPHPR IPLPRDLYGS GRSNSAGLDL ANEHRLASLS SSLLNSALHK WQALPMLEQP
VAEGEMQPVV NPAEPKDIVG YVREASDAEV QQALTSAINN APIWFATPPQ ERAAILERAA
VLMESQMPTL MGILVREAGK TFSNAIAEVR EAVDFLHYYA GQVRDDFDNE THRPLGPVVC
ISPWNFPLAI FTGQIAAALA AGNSVLAKPA EQTPLIAAQG VAILLEAGVP PGVIQLLPGR
GETVGAALTT DERVRGVMFT GSTEVATLLQ RNIASRLDPQ GRPTPLIAET GGMNAMIVDS
SALTEQVVID VLASAFDSAG QRCSALRVLC LQEEVADHTL TMLRGAMSEC RMGNPGRLTT
DIGPVIDAEA KENIERHIQA MRAKGRTVYQ AVRENSEDAR EWRHGTFVPP TLIELDSFDE
LKKEVFGPVL HVVRYNRNEL DKLVEQINAS GYGLTLGVHT RIDETIAQVT GSAKVGNLYV
NRNMVGAVVG VQPFGGEGLS GTGPKAGGPL YLYRLLSSRP QDAVGVTFAR QDAERPLDAQ
LKTLLEKPLQ ALQQWAAGRP ELQALCQQYS EQAQSGTQRL LPGPTGERNT LTLMPRERVL
CVADNEQDAL IQLAAVLAVG CEVLWPDSAL QRDLAKKLPR EVSERIRFAK AEQLPGQAFD
AVIYHGDSDQ LRELCEQVAA RDGAIVSVQG FARGETNLLL ERLYIERSLS VNTAAAGGNA
SLMTIG
//
