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Database: UniProt
Entry: A0A0B2BYV5_9SPHN
LinkDB: A0A0B2BYV5_9SPHN
Original site: A0A0B2BYV5_9SPHN 
ID   A0A0B2BYV5_9SPHN        Unreviewed;      1040 AA.
AC   A0A0B2BYV5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=PK98_13395 {ECO:0000313|EMBL:KHL24871.1};
OS   Croceibacterium mercuriale.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL24871.1, ECO:0000313|Proteomes:UP000030988};
RN   [1] {ECO:0000313|EMBL:KHL24871.1, ECO:0000313|Proteomes:UP000030988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Coronado {ECO:0000313|EMBL:KHL24871.1,
RC   ECO:0000313|Proteomes:UP000030988};
RA   Coil D.A., Eisen J.A.;
RT   "Draft genome sequence of Kirrobacter mercurialis.";
RL   Submitted (NOV-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:KHL24871.1}.
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DR   EMBL; JTDN01000002; KHL24871.1; -; Genomic_DNA.
DR   RefSeq; WP_039097336.1; NZ_JTDN01000002.1.
DR   AlphaFoldDB; A0A0B2BYV5; -.
DR   STRING; 1572751.PK98_13395; -.
DR   OrthoDB; 9812625at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000030988; 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; 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:UP000030988};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN          55..168
FT                   /note="Proline dehydrogenase PutA"
FT                   /evidence="ECO:0000259|Pfam:PF14850"
FT   DOMAIN          177..478
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   DOMAIN          562..1018
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        796
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT   ACT_SITE        830
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ   SEQUENCE   1040 AA;  111287 MW;  7FAF334F9F43FF4C CRC64;
     MIDRSALRTA YRQDEAACIA ERLRQAAPAR EAHGEARALA IRLVEGARQR KASGLDAFLQ
     SYGLGTQEGI ALMCLAEALL RVPDADTADA LIHDKLAGID WSEHLGESSS TFVNAATFSL
     MLTGEVLRGG SKADAGFASS LRRAVGRLGE PVIRQATLQA MRILGGQFVF GRDMEEALKR
     ADPERRRGLT HSFDMLGEAA MTFADATRYR DSYMAAIRRL ARESAAGVAD SPGISVKLSA
     LYPRYDYLHA EVARDALVPI VRELAVAARD ADIHFTIDAE EAERLELSLD IIEVLVADDA
     LFRRADGRQW EGFGLALQAY QKRAVPLCSW VASLARAHGR RLMVRLVKGA YWDAEVKQSQ
     VGGFADYPVF TRKIATDVSY LACAARLLAA ADVLYPAFAT HNAYTIGAIE ALAQDQGNPD
     FEFQRLHGMG EDVYSALAAE GHSRRVRIYA PVGGHKELLA YLVRRLLENG ANSSFVNRMA
     DAAIPAADLA TDPVAELAAL VPQRNPSIPL PTDIFPGRRN SAGVDLADPL VREPLLDRLA
     ALDAREWGAA PTVVAEAAGA ADRTRPVMSP HDGTLVGHVL EAEPADVDAM LARGTAAQIA
     WDGAGGEYRA RLLERAADLF EEHTDEILEL CRREAGKTLP DAVLELREAV DFLRFYAQEA
     RRHFTGNGLL LPGPTGEENR LRLHGRGLFV TISPWNFPLA IFIGPAAAAL AAGNSVIAKP
     AEQTPLIAAF AVQLCHAAGI PDDVLQLAPG DGRVGGMLTG DPRVAGVAFT GSTATAHLIN
     RALAMRPGPI GQFIAETGGQ NALIVDSSAL PEQVTRDVMS SAFQSAGQRC SALRVLYLQE
     DIADSMLAMI RGAFDALQIG DPALLATDVG PVIDRQAQGQ LNDHLAEMRV AGRNVWQAVV
     PPTCAHGSYV APAIVEIDAI GDLQAENFGP VLHVARFRAG QLADVVEQIN ATGYGLTLGL
     HSRIEGNRRL VERRARVGNF YVNRNQIGAV VGSQPFGGEG LSGTGPKAGG PHYLARFATE
     RVTTVDTTAA GGNATLLANL
//
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