ID R4YV58_OLEAN Unreviewed; 1063 AA.
AC R4YV58;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=OLEAN_C34480 {ECO:0000313|EMBL:CCK77624.1};
OS Oleispira antarctica RB-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Oleispira.
OX NCBI_TaxID=698738 {ECO:0000313|EMBL:CCK77624.1, ECO:0000313|Proteomes:UP000032749};
RN [1] {ECO:0000313|EMBL:CCK77624.1, ECO:0000313|Proteomes:UP000032749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23877221; DOI=10.1038/ncomms3156;
RA Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N.,
RA Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R., Langer I.,
RA Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S., Ciordia S.,
RA Singer A., Kagan O., Egorova O., Petit P.A., Stogios P., Kim Y.,
RA Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P., Reva O.N.,
RA Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A., Yakunin A.F.,
RA Yakimov M.M., Golyshina O.V., Reinhardt R., Golyshin P.N.;
RT "Genome sequence and functional genomic analysis of the oil-degrading
RT bacterium Oleispira antarctica.";
RL Nat. Commun. 4:2156-2156(2013).
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; FO203512; CCK77624.1; -; Genomic_DNA.
DR AlphaFoldDB; R4YV58; -.
DR STRING; 698738.OLEAN_C34480; -.
DR KEGG; oai:OLEAN_C34480; -.
DR PATRIC; fig|698738.3.peg.3588; -.
DR HOGENOM; CLU_005682_1_0_6; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000032749; Chromosome.
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; 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:UP000032749};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 76..188
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 197..495
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 584..1042
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 820
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 854
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1063 AA; 117502 MW; A27957E1E4708053 CRC64;
MNSFDASKML LESEQTISSS QWFERIVNHY AVDEDVLMPE LCLLAEPNQE IRYKTENRAR
VLIDNIRSQG DIAHAVDKLL QEYSLDNEEG VILMCLAEAL MRIPDDDTAD ALIRDKLSEA
EWDEHLGKSE SLLVNASTWG LMLTGKVIGV GGKKKTPANL LARLIKRAGE PVIRSAMHQA
MRIMGKQFVL GRTIDEAIKQ SKSYRAKGYT YSFDMLGEAA FTDVDAEGYF ESYLSAIRSL
AKSHDVWRED RPQPSISIKL SALFPRYEEA HAAAVMDELY QRVLTLITEA RQLNIAITID
AEEADRLELS LRLFSKLYHN PDVQGWGLFG LVVQAYSKRA LPVLGYLASL ARAQGDEIPI
RLVKGAYWDT EIKHAQQLGL ADYPVFTRKE NTDVSYMACA RYLLSSATDG CIYPQFASHN
AHTVAAVTEM AADNPTRLFE FQRLHGMGDA LYDTLLSEST VNVRIYAPVG AHKDLLPYLV
RRLLENGANS SFVHRLVDAN TPVTDLITSP IEQAQRHGIY RNIKIPRPGE LFTPIENGQR
RNSQGYNLAV EFEREPLLAD VQQFSKTHWS FEPIINGKKV KEATQETHII HSPYDHEQVV
GELHWATAEH AKQALECADQ AWFEWNQTPV IERAACLDRT ADLLEQHTAE LIALCTREAG
KTLQDGIDEI REAVDFCRYY AQQARQEMAS PTLLPGPTGE SNEHYYAGRG TFLCISPWNF
PLAIFLGQIS AALVTGNCVL AKPAEQTSLI AGRTIELMHE AGIPGNVLHF LPGAGATIGD
ALLSDERLVG IVFTGSTATA KHINMTLAQR DGAIPTFIAE TGGQNAMIVD STSLPEQVVA
DVMDSAFSSA GQRCSALRVL YVQDDIADRV IELITGALQR FVVGNPELYA TDCGPVIDSR
AQLGLLTHCE HWQAQGKLLA QALNHDDLAK GFYVLPTMIA IDSISELKKE EFGPILHICR
FEADELDQVI NDINQTGYGL TLGIHSRNEV TAAYIESRVR VGNCYVNRNQ VGAVVGVQPF
GGQGLSGTGP KAGGPNYLKR FATERVRTIN TTAVGGNASL LSQ
//
