ID A0A246WKC5_9BURK Unreviewed; 1229 AA.
AC A0A246WKC5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:OWY26674.1};
GN ORFNames=CEJ42_23220 {ECO:0000313|EMBL:OWY26674.1};
OS Herbaspirillum robiniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=2014887 {ECO:0000313|EMBL:OWY26674.1, ECO:0000313|Proteomes:UP000197596};
RN [1] {ECO:0000313|EMBL:OWY26674.1, ECO:0000313|Proteomes:UP000197596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ10 {ECO:0000313|EMBL:OWY26674.1,
RC ECO:0000313|Proteomes:UP000197596};
RA Fan M., Lin Y.;
RT "Herbaspirillum phytohormonus sp. nov., isolated from the root nodule of
RT Robinia pseudoacacia in lead-zinc mine.";
RL Submitted (JUN-2017) 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:OWY26674.1}.
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DR EMBL; NJGU01000017; OWY26674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246WKC5; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000197596; 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; 1.20.5.460; 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; 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 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 PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF53720; ALDH-like; 2.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR SUPFAM; SSF81935; N-terminal domain of bifunctional PutA protein; 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 Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 31..77
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 86..197
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 207..503
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 587..1030
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 811
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 845
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1229 AA; 133168 MW; 363C1174744B9A2C CRC64;
MTTAAPTPVS AASSGLPFGA FHAEVMHAPD PLRAAITAAY RRDEPEAVQW LLGQVKSEAA
WQEQTQQLAR KLVQQVREKR TRSSGVDALM HEFSLSSEEG VALMCLAEAL LRIPDRQTAD
RLIADKISKG DWRKHLGESP SLFVNAATWG LLITGKLVST SSESSLGSAI TRLIGRGGEP
LIRKGVDLAM RMLGNQFVTG QTIEEALDNS RENEKRGYRY SYDMLGEAAL TMHDADAYYK
SYEDAIHAIG RASNGRGIKD GPGISVKLSA LHPRYSRAQQ SRVMSELLPR LKQLLLLAKQ
YNIGLNIDAE EADRLELSLD MMEVLVADPD LAGFEGIGFV VQGYQKRCPF VIDYLVDLAR
RNKRRLMIRL VKGAYWDSEI KRAQVDGLEG YPVYTRKVHT DLSYLTCAQK LLASTDVIYP
QFATHNAHTL AAIWNWARLH NIDDYEFQCL HGMGETLYDQ VVGKENLGKA CRVYAPVGSH
QTLLAYLVRR LLENGANSSF VNQIVDEAVA LDKLVADPIE TVRAQGGQPH PSIALPHKLY
GQERKNSAGI DLSNEDRLRQ LDQLFARMAD RRWQAAPLIA GAVAAADRQA VHNPADRREL
VGEVIEATLP DVETALAAAT DYAPQWQATP AAQRAAMLER GADLLEDNIA ELMALAVREA
GKSLPNAIAE VREAVDFLRY YAIASRHDGN ALAYGPVVCI SPWNFPLAIF IGEVSASLAA
GNVVLAKPAE QTALIAHRAV QLLHEAGVPL AALQLLPGRG ETVGAALTSD ERVKGVIFTG
STEVAQLINR TLAKRNHGEN GEHGEVPLIA ETGGQNALIV DSSALAEQVV VDVLSSAFDS
AGQRCSALRI LCLQEDIAER TLEMLKGAMA ELRVGRPDRL ATDIGPVIDA EAQQNLLNHI
ERMRGSAKSV HQLTLDAACE HGTFVPPTVI EIADLSQLQR EVFGPVLHVL RYRRDQLSQL
VDAINATGYG LTLGVHSRID ETIDFVASRA HVGNIYVNRN IVGAVVGVQP FGGEGKSGTG
PKAGGPLYLK RLQRNPQLQE ELTRAQPAAV PNTLLDSLLD WARTHGHERL AVTGQRYHGD
SLLQRSLLLP GPTGERNTLA FAPRGLVLCV AASVGTLLNQ LAAAFATGNT VVVDGASAVY
IPAGLPQQVR AAIRQSDRLE GEPLQAALVD SHSAQAWRAK LAAREGALVP LVVCSEDTAI
ALWRLLAERA LCVNTTAAGG NASLMTISV
//
