ID A0A1G7WQY4_9BRAD Unreviewed; 999 AA.
AC A0A1G7WQY4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216338_1002303 {ECO:0000313|EMBL:SDG74316.1};
OS Bradyrhizobium sp. Rc2d.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855321 {ECO:0000313|EMBL:SDG74316.1, ECO:0000313|Proteomes:UP000198770};
RN [1] {ECO:0000313|EMBL:SDG74316.1, ECO:0000313|Proteomes:UP000198770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rc2d {ECO:0000313|EMBL:SDG74316.1,
RC ECO:0000313|Proteomes:UP000198770};
RA de Groot N.N.;
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; FNCU01000002; SDG74316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7WQY4; -.
DR STRING; 1855321.SAMN05216338_1002303; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000198770; 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 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; 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 PIRSF; PIRSF000197; Bifunct_PutA; 2.
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 Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 58..167
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 178..470
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 540..981
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 758
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 792
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 999 AA; 107557 MW; 3090FB2292CBE1CA CRC64;
MPNIPPPFSA PYAPDDSDIA ARLLPASHLS PPQEARIDRT ATRLIEAIRK RDDRLGGVED
MLREFALSTK EGLALMVLAE ALLRVPDART ADQFIEDKLG EGDFIHHETK STAFLVNASA
WALGISARVI QPGETPDGTI GRLVKRLGAP AVRTATRQAM RLMGNHFVLG ETIEQALERG
RPRSGQKPRY SFDMLGEAAR TAADATRYFD AYASAIETIG KTAGSHPLPD RPGISVKLSA
LHPRFEAISR ERVMRELVPL LLDLAQRAKA HDLNFTVDAE EADRLELSLD VIAATLADPS
LAGWDGFGLA IQAYQKRASA VIDYVEALAR AHDRKLMVRL VKGAYWDTEI KRAQERGLDG
YPVFTRKAMT DLNYVACASK LLGLRPRIFP QFATHNALTV ATVLELAGKS GGFEFQRLHG
MGEALYEQLA KDHPEIAYRT YAPVGSHRDL LAYLVRRLLE NGANSSFVAQ AADYRVPVLA
LLQRPADAIE RPQQAAHPKI PLPRDLFAPE RRNSRGVEFG EHAALDRLLA DVKAETADLM
PITDTTPDQA NAAVAAARAG FVAWSRTPAA ARAAALEQAA HLLESRSAHF IALLQAEGGK
TLDDALSELR EAADFCRYYA AQGRKLFGVD AAMPGPTGES NALAMRGRGV FAAISPWNFP
LAIFLGQVTA ALMAGNSVVA KPAEQTPRIA REAVALLHEA GIPKSALHLV TGDGHIGAVL
TAHADIAGIV FTGSTEVARQ INRTLAAKDG PIVPLIAETG GINAMIADAT ALPEQVADDV
VTSAFRSAGQ RCSALRLLFV QEDVADRMIE MIAGAARELK IGDPSDVATH VGPVIDREAK
QRLDAHIARM KTEARLHFAG HAPEGCFVAP HIFELKDAGQ LTEEVFGPIL HVVRYRPETL
ERVLQAIERT GFGLTLGVHS RIDDTIEAII DRVRVGNIYV NRNMIGAVVG VQPFGGNGLS
GTGPKAGGPH YLARFATEQT VTINTAAAGG NAALLAGEE
//
