ID A0A081G2R0_9GAMM Unreviewed; 1039 AA.
AC A0A081G2R0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ADIMK_0767 {ECO:0000313|EMBL:KEA65065.1};
OS Marinobacterium lacunae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA65065.1, ECO:0000313|Proteomes:UP000028252};
RN [1] {ECO:0000313|EMBL:KEA65065.1, ECO:0000313|Proteomes:UP000028252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK27 {ECO:0000313|EMBL:KEA65065.1,
RC ECO:0000313|Proteomes:UP000028252};
RA Singh A., Pinnaka A.K.;
RT "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT collected from Kochi backwaters in Kerala, India.";
RL Submitted (APR-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:KEA65065.1}.
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DR EMBL; JMQN01000013; KEA65065.1; -; Genomic_DNA.
DR RefSeq; WP_036183829.1; NZ_JMQN01000013.1.
DR AlphaFoldDB; A0A081G2R0; -.
DR STRING; 1232683.ADIMK_0767; -.
DR PATRIC; fig|1232683.4.peg.759; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000028252; 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:UP000028252};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 73..187
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 197..489
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 577..1032
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 809
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 843
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1039 AA; 114685 MW; 4D5CE33CFB4DA2ED CRC64;
MFKAIDTLEP GYIRQPMDLL WQQISPLYAA DEDQVLRELM PLAEPHGDEL TSIEARATRL
IEQVRADDGA IHMIDALLLE YSLDTREGIL LMCLAEALMR IPDTDTADAL IRDKLSIADW
KRHLSQSESL LVNASTWGLL LTGKVVTLDE REDGTPSGVI NRLVNRLSEP VIRKVMQQAM
KIMGHQFVLG RDMPEATKRG REYRERGYTY SFDMLGEAAL TAADATKYYT DYTRAIDHVG
NLPDIGSSPR PSVSIKLSAL HPRYEVLQEA RVMEELAERV FLLIRRARPL NVALTIDAEE
ADRLELSLKL FEKLYRSQET LGWDGLGLVV QAYSKRALPV LTWLAALSLD VGDRIPVRLV
KGAYWDSEIK VCQQRGLSGY PVYTRKEATD VAYLACARFL LGEHIRGLIW PQFASHNAHT
VASIMTLAKH ADFEFQRLHG MGDALYDQVL DTAGVTVRIY APVGNHKDLL PYLVRRLLEN
GANSSFVHRL VDQRCPISDL IQHPWQVLHS RDTLHNPNIP LPEAIFGAER NASKGPNILI
ESQWLPFSEK VGECLEQCWQ ADPIIDGRAT PGQALHSDVR SPANRDILVG QVTYADHAQT
IAAIDAAERF LPVWQSTSVT ERTAPLRRLA DLLEQHMEEL VALCHQEAGK TIQDSIDEVR
EAVDFCRYYP ARAEALYEEH LELGTLSGDT AHWQRQGRGI FVCISPWNFP LAIFLGQISA
ALVTGNCVIA KPAEQTSLIA ARAIELMLQA GIPGGAIQFL PGEGTTVGAA LTSDPRIAGV
AFTGSTETAQ RINRSLSRRE CEPATLIAET GGQNAMIVDS TALPEQVVKD AVLSGFASAG
QRCSALRVLC VQNDIADRII ELLKGAMAEL TLGDPALLST DIGPVIDEQA QSSLLEHIAR
MKEHAKVLAQ TPMSGCTKRG MYVPPTAIEI SRIDQIGREQ FGPIIHVLRY SARHLDQLID
QINAAGYGLT LGIHSRNERT AAHIEARARV GNTYINRNQI GAVVGVQPFG GQGLSGTGPK
AGGPYYLPRF TRLIPVDKA
//
