ID A0A074JIU7_9RHOB Unreviewed; 1139 AA.
AC A0A074JIU7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=TP2_02420 {ECO:0000313|EMBL:KEO56404.1};
OS Thioclava pacifica DSM 10166.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353537 {ECO:0000313|EMBL:KEO56404.1, ECO:0000313|Proteomes:UP000027432};
RN [1] {ECO:0000313|EMBL:KEO56404.1, ECO:0000313|Proteomes:UP000027432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10166 {ECO:0000313|EMBL:KEO56404.1,
RC ECO:0000313|Proteomes:UP000027432};
RA Lai Q., Shao Z.;
RT "Thioclava pacifica DSM 10166 Genome Sequencing.";
RL Submitted (JUL-2013) 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:KEO56404.1}.
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DR EMBL; AUND01000001; KEO56404.1; -; Genomic_DNA.
DR RefSeq; WP_038072887.1; NZ_AUND01000001.1.
DR AlphaFoldDB; A0A074JIU7; -.
DR STRING; 1353537.TP2_02420; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000027432; 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; IPR041349; PRODH.
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:UP000027432};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 15..50
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 58..168
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 177..469
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 545..976
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 1139 AA; 121873 MW; A59E3EFE3C6182CB CRC64;
MRVSFDQFTH EAKFADEAEL LSRLQAQADL SAATRAQISA RAATLVRRIR TEAKPTLMEH
FLAEYGLSTQ EGVALMCLAE AMLRVPDAET IDALIEDKIA PSDWGKHMGT ASSSMVNAST
WALMLTGRVL EDEKPGMEGV LRGAIRRLGE PVIRAAVSRA MKEMGRQFVL GETIENALSR
AKKLEDRGYT YSYDMLGEAA RTAADAKRYA KDYANAIAAI AKVCKDRPVA ENPGISVKLS
ALHPRYEVAK EARVMAEIVP VMRDLARAAK AGNMGLNIDA EEQDRLVLSL KIIEEVLSDP
ELAGWDGFGV VVQAYGKRAS LVIDWLGALA EKLDRKIMVR LVKGAYWDTE MKLAQVEGLP
DFPLFTTKAA TDVSYLANAR KLFSYTDRIY PQFATHNAHS VAAILEMAEG RPFEFQRLHG
MGERLHEIVH REEGTRCRIY APVGAHRDLL AYLVRRLLEN GANSSFVHQI VDEDVAPETI
AEDPFVQLAK AERSVMLHHP SRIFGAGRIN SAGFDLTDEE TLARIEAARD VAIPDAGPLV
AGEASGQTVA VRNPATGEDL AKVTEADAAC VASAIDAARA WQAPVSERAA ILRRVADLYE
ENFGPFFAVL AKEAGKSQLD AVGELREAVD FLRYYAAQAE EQDPIPRGIF AAISPWNFPL
AIFTGQISAA LAAGNGVIAK PAEQTPLVAA IAVRLMHEAG VPRDVLQLLP GQGETVGAAL
TSNPKIAGVA FTGSTETAKM IRRAMAENLD PHAPLIAETG GLNAMIVDST ALPEQATRDI
IASAFQSAGQ RCSALRCLYV QEDVADGLIA MIKGAMDELS LGDPWVLSTD VGPVIDAEAQ
ADIAEYIAKA EAEGRVLHKL DAPAQGHFIA PTLIKVSGIA DLEREVFGPV LHVATYRAED
IEKVYAAINA TGYGLTAGLH SRIDSRVQEV SDALHVGNLY VNRNQIGAVV GSQPFGGEGL
SGTGPKAGGP LYLTRFARAP DAPSKEGEWG HKADLDTLRK RLAKAAAKAE AAGPLDTLEL
PGPTGEANTL RRFARGPILC LGPGEAAQVA QIKAVEKLGG IAVGSDGKIA PEVIETLGDI
AGVIWWGGEP RAYVQALAKR DGPILSLITG AVQKTDVVHE RHLCVDTTAA GGNAALLAG
//
