ID Q2NTK7_SODGM Unreviewed; 1314 AA.
AC Q2NTK7;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 121.
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:CRL45234.1};
GN OrderedLocusNames=SG1243 {ECO:0000313|EMBL:BAE74518.1};
GN ORFNames=SGGMMB4_02821 {ECO:0000313|EMBL:CRL45234.1};
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE74518.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE74518.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Morsitans {ECO:0000313|EMBL:BAE74518.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000001932};
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
RN [2] {ECO:0000313|EMBL:CRL45234.1, ECO:0000313|Proteomes:UP000245838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:CRL45234.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000245838};
RA Goodhead I.;
RL Submitted (MAY-2015) 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}.
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DR EMBL; AP008232; BAE74518.1; -; Genomic_DNA.
DR EMBL; LN854557; CRL45234.1; -; Genomic_DNA.
DR RefSeq; WP_011411072.1; NZ_LN854557.1.
DR STRING; 343509.SG1243; -.
DR KEGG; sgl:SG1243; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG3905; Bacteria.
DR eggNOG; COG4230; Bacteria.
DR HOGENOM; CLU_005682_1_0_6; -.
DR OrthoDB; 9812625at2; -.
DR BioCyc; SGLO343509:SGP1_RS11100-MONOMER; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000001932; Chromosome.
DR Proteomes; UP000245838; Chromosome sggmmb4_Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
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:0043565; F:sequence-specific DNA binding; IEA:UniProt.
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 CDD; cd22233; RHH_CopAso-like; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR Gene3D; 1.10.1220.10; Met repressor-like; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 1.
DR Gene3D; 1.20.5.550; 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; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR025703; Bifunct_PutA.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR041349; PRODH.
DR InterPro; IPR024090; PRODH_PutA_dom_I.
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 InterPro; IPR048798; PutA_RHH.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
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 Pfam; PF21775; PutA_1st; 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 SUPFAM; SSF47598; Ribbon-helix-helix; 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 Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT DOMAIN 11..42
FT /note="PutA RHH"
FT /evidence="ECO:0000259|Pfam:PF21775"
FT DOMAIN 88..132
FT /note="Proline utilization A proline dehydrogenase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18327"
FT DOMAIN 144..255
FT /note="Proline dehydrogenase PutA"
FT /evidence="ECO:0000259|Pfam:PF14850"
FT DOMAIN 264..565
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 657..1096
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 879
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 913
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1314 AA; 143597 MW; E3033E6F6E47A6F5 CRC64;
MGTTTMGVKL DDEARERIKQ AARQLDRTPH WLIKQAIFHY LDALEQGATP GLPLPAAEAD
DTLKVVSDEP RQPFIDLAEQ ILPQSITRAA VTAAWRRPET EAVPWLLEQA RHPAPMAETI
QTLAGKLANQ LRHQKRSGGR AGIVQDLLQE FSLSSQEGIA LMCLAEALLR IPDKATRDAL
IRDKISNGNW QTHLGRSQSL FVNAATWGLL FTGKLVATHN EASLSRSLNR IIGKSGEPLI
RKGVDMAMRL MGEQFVTGEH IGEALANAHR LEQQGFRYSY DMLGEAALTE EDAQAYLLSY
QQAIHAIGKA SSGRGIYEGP GISIKLSALH PRYCRAQYER VMAELYPRLL RLTLLARQYD
IGLNIDAEEA DRLEISLDLL ARLCFEPALA GWNGIGFVIQ AYQKRCPQVI DELIDLAKRS
QRRLMIRLVK GAYWDSEIKR AQIEGLEDYP VFTRKVYTDL SYLACARKLL SVPHYIYPQF
ATHNAHTLAA IYHFAGQNYY PGQYEFQCLH GMGEPLYEQV VGKVAEGKLN RPCRIYAPVG
SHETLLAYLV RRLLENGANT SFVNRIADSA VPLEQLIADP VQEVTQLAVR EGRAGLPHPK
IPLPRDLYGA QRRNSAGLDL ANEHRLASLS AALLNVEHQT WQAAPVVVTE IGDGAVQKVL
NPADHRDVVG ECRQASSEEV AHALAAAVHH GSLWSATPPA DRAAVLKEAA NRLETDMQPL
IGLLVREAGK SFSNAVAEVR EAVDFLRYYA CQIAQDFDND NYRPLGPVVC ISPWNFPLAI
FLGQIAAALA AGNTVLAKPA EQTPLIAARA VALMLEAGVP LGVLQLLPGA GETVGAALVA
DPRVRGVMFT GSTQVARLLQ TTLAARLDPQ GRPIPLIAET GGLNAMLVDS SALTEQVIID
VVTSAFDSAG QRCSALRLLC IQEDVAERTL RMLRGAMAEY TLGNPERLAT DIGPVIDSSA
KAAIDSHITA MRERGYTVWQ TPAAEAAGDI QGTFVPLTLI ELDSIEALTQ EVFGPVLHVV
RYQRRELDSI IDQINGSGYG LTLGLHTRID ETIQRVTERA HVGNCYINRN IVGAVVGVQP
FGGEGLSGTG PKAGGPLYLY CLLSQRRDDA LLPSLQALDA VHAPDFTRRE ILQQAHPALV
AWMETHQPTL VAQCRHLGEI SQAGSVRLLT GPTGEQNSYR LLPREHILCL ADQDPDLLLQ
LAAITSIGAR ALWAESPQSR RLFTTLPDSV RQRITLLADW TQEDVRLDAV LFHGDSDQLR
NLAQTLSKRP GPLITVQGNA RGDGQIALER LLIERAISVN TAAAGGNASL MTIG
//
