ID A0A014NXP4_9BURK Unreviewed; 1279 AA.
AC A0A014NXP4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:EXU78645.1};
GN ORFNames=AX13_11755 {ECO:0000313|EMBL:EXU78645.1};
OS Comamonas aquatica DA1877.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU78645.1, ECO:0000313|Proteomes:UP000020766};
RN [1] {ECO:0000313|EMBL:EXU78645.1, ECO:0000313|Proteomes:UP000020766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU78645.1,
RC ECO:0000313|Proteomes:UP000020766};
RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA Caudy A.A., Walhout A.J.;
RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT Gene Expression and Life History Traits.";
RL Submitted (JAN-2014) 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: 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXU78645.1}.
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DR EMBL; JBOK01000031; EXU78645.1; -; Genomic_DNA.
DR RefSeq; WP_043387270.1; NZ_JBOK01000031.1.
DR AlphaFoldDB; A0A014NXP4; -.
DR STRING; 225991.MA05_12380; -.
DR PATRIC; fig|1457173.3.peg.3502; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000020766; Unassembled WGS sequence.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000020766};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 11..42
FT /note="PutA RHH"
FT /evidence="ECO:0000259|Pfam:PF21775"
FT DOMAIN 92..137
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 147..257
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 267..567
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 652..1089
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 874
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 908
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1279 AA; 138359 MW; 36899732952099DE CRC64;
MATTTIGIKV DELMRDRLKA AAQQLGCTPH WLHKQALHSY LEAIELGKPL PELQYLGSTQ
PGGELLEPEA LADASQPYAP FYALAQDVQP QSVLRAAITA AYRRPETECI PLLLAPATST
NPTGVAQLAT RLVQALRDKR LKKTSGVEAL VQEYSLSSQE GVALMCLAEA LLRIPDRATR
DALIRDKVSK GDWKSHTDSP SVFVNAATWG LMITGKLVAV HSEQKLSSAL TRLIARGGEP
LIRQGVNTAM RMMGEQFVTG QTIAAALANS RKLEDKGFRY SYDMLGEAAT TEEDALRYLQ
SYEQAIHAIG QASQGRGIYE GPGISIKLSA LHPRYSRAQR ERVMQELYPR LLKLAELARQ
YDIGLNIDAE EADRLEISLD LLEQLCFAPS LAGWNGIGFV VQAYQRRAFF VLDWIIDLAR
RSKHRLMVRL VKGAYWDSEI KRAQVDGLED YPVYTRKLHT DVSYLACARK LLGAPEAIFP
QFATHNAHTL ASIYHMAGNN YYRGQYEFQC LHGMGEGLYE EVVGDIAQGK LARPCRIYAP
VGTHETLLAY LVRRLLENGA NSSFVHQIGD ETVDIAQLVT DPVAAAQALS PLGRPHDRIP
APAQLYAAQG RSNSSGLDLS NEQRLASLSA ALLSSSAPWR AEPAHAAHLP AQPVNNPAHA
GDVLGEVRMA GAAEVAHTMA QAQHAAPIWQ ATPVQARAEA LLRAADLMQA QLQPLMGLLC
REAGKTLPNA ISEVREAIDF LRYYAQQAVQ HLNNGSHRPL GVVVCISPWN FPLAIFAGQI
AAALAAGNVV IAKPAEQTNL IAAQAVALLH QAGIPEHALQ LLPGDGETVG EALVAHPSTD
AVVFTGSHPV AQHIHRRLSQ RLGSHGKPVP LIAETGGINA MVVDSSALSE QVVGDVLMSA
YDSAGQRCSA LRLLCLQEDS ADHVLRMLRG AMQELRVGNP DQLATDVGPV IDAQARADIE
AYIEQMRGQG HTVTRLELPA ECRHGHFVAP TLIEVSRVQD LSREVFGPVL HVLRYARKDM
DALLQDINSL GFGLTFGVHT RLDETVAHVS ERIHAGNIYV NRNIVGAVVG VQPFGGEGLS
GTGPKAGGPL YLFRLLAQAP ALEQLPVLTA RGPQTLNVAA GQQVLLDGPT GETDQYLLQA
RGAIWCLPLT VDGLQAQWQA CQATGNTLLL QDTPALRALV AQWQQAQPAA QAAALHWADA
AQIAQLPLQA ALAESDTDAL LPLQQQLSAR SGPLLLVQGL TTEEIRNGER YRQERLLREI
SISTNTTAAG GNASLMMVG
//
