ID D5AN87_RHOCB Unreviewed; 1127 AA.
AC D5AN87;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 Name=putA {ECO:0000313|EMBL:ADE86377.1};
GN OrderedLocusNames=RCAP_rcc02647 {ECO:0000313|EMBL:ADE86377.1};
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE86377.1, ECO:0000313|Proteomes:UP000002361};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB1003;
RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADE86377.1, ECO:0000313|Proteomes:UP000002361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC {ECO:0000313|Proteomes:UP000002361};
RX PubMed=20418398; DOI=10.1128/JB.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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; CP001312; ADE86377.1; -; Genomic_DNA.
DR RefSeq; WP_013068356.1; NC_014034.1.
DR AlphaFoldDB; D5AN87; -.
DR SMR; D5AN87; -.
DR STRING; 272942.RCAP_rcc02647; -.
DR GeneID; 31491470; -.
DR KEGG; rcp:RCAP_rcc02647; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR HOGENOM; CLU_005682_1_0_5; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000002361; 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 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:UP000002361};
KW Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 57..167
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 176..468
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 548..973
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 757
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 791
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1127 AA; 117298 MW; D850D5315083487B CRC64;
MTDLSALGPK AKFAPEAEVL QALVAQAALP QPQLDRIAAR GADLVARIRA EAKPSLMEHF
LAQYGLSTRE GVALMCLAEA MLRVPDTATI DALIEDKIAP SDWGKHLGTA ASSLVNASTW
ALMLTGKVLD DGAGGIAGTL RGAMRRLGEP VIRAAVGQAM REMGRQFVLG ETIEKALERA
EKREAEGYTF SYDMLGEAAL TAADAERYRL AYAQAITAIG KAATRGSIAA NPGISIKLSA
LHPRYEVAQE ARVMAELVPV VRDLARAAAR AGIALHIDAE EQDRLALSLR VMAAVIADPE
TAGWEGFGAV VQAYGKRAGA AIDALAAMAR AAGRRINIRL VKGAYWDAEM KRAQVEGHPG
FPLFTSKTGT DVAYICLAAK LFGLNDCIYP QFATHNAHTV AAVLEMAAGR PFEFQRLHGM
GARLHDIVLR ETGGRCRIYA PVGAHRDLLA YLVRRLLENG ANSSFVNQIV NESVPPAEVA
ACPFAALPTA RAPRGLLAPA DLFGAGRVNA QGFDLSDPEV LARIEAARDV TLPDAAPIVA
GPVSGTLRPV RNPATGAVVA QVTEADAATV ALALDAAQVW SAPAATRAAV LCRAADLYEE
NFGPIFAALA QEAGKTLGDA VSELREAVDF LRYYAAEGAA DTRPPRGAVV AISPWNFPLA
IFTGQVAAAL MAGNAVLAKP AEQTPIIAAL AVRLLHQAGV PETALQLLPG DGPTVGAALT
RDPRVAGVVF TGSTETAQII ARAMAAHLAP GTPLIAETGG LNAMVVDSTA LPEQAVRDVV
ASAFRSAGQR CSALRCLYVQ DDIAPHLIGM LKGAMEELVS GDPARLSTDV GPVIDAEAKA
GIETYLAANK ARILHRSTAP EGGHFVAPAL LQVGGIADLE REIFGPVLHL ATFAAEDLPA
VIAAINARGY GLTFGLHSRI DARVETVAET IRAGNIYVNR NQIGAVVGSQ PFGGEGLSGT
GPKAGGPLYL NRFYAPEPVV AVGGWTEAAT PILPEARETQ LDEIFLPGPT GELNRLTRHQ
RGPILCLGPG AEAASAQAAA VVALGGQAVQ ASGAVSPKAL ETLTPLAGVL WWGAAEMGRA
YAQALAVRPG PLVPLITAKP DLAHVAHERH LCVDTTAAGG NAALLAG
//
