ID A0A1H7BVW2_9SPHN Unreviewed; 1203 AA.
AC A0A1H7BVW2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ORFNames=SAMN05428950_103312 {ECO:0000313|EMBL:SEJ81699.1};
OS Sphingomonas sp. OV641.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1881068 {ECO:0000313|EMBL:SEJ81699.1, ECO:0000313|Proteomes:UP000199191};
RN [1] {ECO:0000313|Proteomes:UP000199191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV641 {ECO:0000313|Proteomes:UP000199191};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNZB01000003; SEJ81699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7BVW2; -.
DR STRING; 1881068.SAMN05428950_103312; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000199191; 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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000199191};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 19..66
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 74..185
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 194..492
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 573..1009
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 795
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 829
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1203 AA; 127780 MW; CAAA924FAC67614A CRC64;
MPTLSPLFAD FAPPVRSATP LRAAITAATR RPEPEALAPL LDEATLPDAI KAQALATATT
LITALRAKHK GTGVEGLVQE YALSSQEGVA LMCLAEALLR IPDDDTRDAL IRDKIAGGDW
RSHIGDGRSL FVNAATWGLV VTGKLTNSVN DRGLAAALTR LIARAGEPVI RRGVDMAMRM
MGEQFVTGET IGEALKRARP LEARGFGYSY DMLGEAATTV ADADRYYRDY ETAVHAIGKA
SAGRGVYAGP GISIKLSALH PRYARAQADR VMGELLPKVR ALALVAKGYD IGFNIDAEEA
DRLELSLDLL ESLSLDPDLA GWNGLGFVIQ AYGKRCPFVI DWIVDLARRA NRRIMVRLVK
GAYWDAEIKR AQVDGQADFP VYTRKIHTDV SYLACARRLL ANRDAVFPQF ATHNAQTLAT
VHAMAGPEFT IGDYEFQCLH GMGEPLYDEV VGPDKLNRPC RIYAPVGTHE TLLAYLVRRL
LENGANSSFV NRIADPEVSI TDLVADPVAV VRATDTPGQK HAGIALPADL YPRRRNSDGI
DLADERTLAG LAETMQAGAH DKWRAASADG QGTPRPVLNP ADHRDIVGTV VEVTPEQASA
AARTAAAAAP AWAAVPAAER AAMLDRAADA MQARMAELIG LTVREAGKSV PNAIGEVREA
IDFLRYYADQ ARRSFGPAHR PLGAVTCISP WNFPLAIFTG QVAAALVAGN TVLAKPAEET
PLIAAQGVAI LHEAGVPSDV LQLVPGDGSI GAALVAAPET AAVMFTGSTE VARLIQRELA
TRLSPEGTPI PLIAETGGQN AMIVDSSALA EQVVADVIAS AFDSAGQRCS ALRVLCLQEE
VADRILTMLR GALQELRIGR TDRLAVDIGP VITAEAQENI TRHIAAMRDR GHKVDSLALS
DETAQGTFVA PTIIELSDIA ELEREVFGPV LHVIRYKRSG LDALIDRINA TGYGLTFGLH
TRLDETIAHV TARVKAGNLY INRNIIGAVV GVQPFGGRGL SGTGPKAGGP LYLGRLVRGA
IEAPAGTSIT ADAAARDLAL WLGNGGDEAT AARVRDIAAA SPLGLETELD GPVGERNLYA
LHPRGRILLL PETREGLMAQ LTAGLATGND LVVDAGLRTD LPAPVAARIH WSADWASEGP
YAGALIEGDA ARVRDLQQRI AALDGPIVLT QAGDYRLEWL VEEVSTSINT TAAGGNASLM
AMT
//
