(data stored in ACNUC7421 zone)

SWISSPROT: B4STH0_STRM5

ID   B4STH0_STRM5            Unreviewed;      1085 AA.
AC   B4STH0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 74.
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   OrderedLocusNames=Smal_0308 {ECO:0000313|EMBL:ACF50013.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50013.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50013.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50013.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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|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|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; CP001111; ACF50013.1; -; Genomic_DNA.
DR   STRING; 391008.Smal_0308; -.
DR   EnsemblBacteria; ACF50013; ACF50013; Smal_0308.
DR   KEGG; smt:Smal_0308; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG0506; LUCA.
DR   eggNOG; COG4230; LUCA.
DR   HOGENOM; HOG000253912; -.
DR   KO; K13821; -.
DR   OMA; VRIYAPV; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000001867; 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:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; 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; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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; IPR005933; Delta1-pyrroline-5-COlate_DH-3.
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   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; SSF51730; SSF51730; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   SUPFAM; SSF81935; SSF81935; 1.
DR   TIGRFAMs; TIGR01238; D1pyr5carbox3; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STH0.
DR   SWISS-2DPAGE; B4STH0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
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|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       43     89       PRODH. {ECO:0000259|Pfam:PF18327}.
FT   DOMAIN       98    211       Pro_dh-DNA_bdg. {ECO:0000259|Pfam:
FT                                PF14850}.
FT   DOMAIN      226    520       Pro_dh. {ECO:0000259|Pfam:PF01619}.
FT   DOMAIN      606   1067       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    840    840       {ECO:0000256|PIRSR:PIRSR000197-1}.
FT   ACT_SITE    874    874       {ECO:0000256|PIRSR:PIRSR000197-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   1085 AA;  116630 MW;  BDBA5CB88586097C CRC64;
     MIKIAKFSIG RTGMNAPFSS PAASDASRPG ALLSPELPAS PNPFRQAITD GWLKDEASHV
     RELLAQARLP AEEQAKVQAL AADLVGRVRV RAKDQGAIEA FMRQYDLGSE EGVLLMCVAE
     ALLRIPDQDT ADKLIRDKLA DADWEKHLGG SDSVLVNAST WGLMLTGKLV QMNDATRADA
     PSAFKRLVGR VGEPVVRLAV RQAMKIMGHQ FVMGRTISEA LSRSHKGDNA SYRYSFDMLG
     EGALTMKDAL RYLEDYRRAI HAIGGDHKAR GGRPDGDVNN APGISIKLSA LYPRYEHAKR
     ERVLKDLVPG VLELAQLARS YGIGCTVDAE ESDRLELSLD IIEQVFSDAS LAGWDGFGVV
     VQAYQKRTPY TIDHLADMAR RAGRRLQVRL VKGAYWDAEI KRAQIEGYPG YPVFTRKQNT
     DVSYLACAKR LFTHADAIYP MFATHNAHTI AAVRSIANGG VYEHQKLHGM GDDLYAEVVP
     ADRLNLPCRV YAPVGSHEDL LPYLVRRLLE NGANSSFVNR ITDERVPIAD LIRDPVEMVA
     SFESIPHPKI PLPVDLLRSQ NHDRKNSMGA NLANDNELRA LAEQLNTAVK PWSAAPLVPG
     ANPAGATQPV TNPADTREVV GQWQAADAAT VQKALANAVA AQPAWNRTPA ASRAAILEHA
     ADQLEARMPE FMALCVKEAG KSLPDGIAEV REAVDFLRYY AKQAREQFSH AEKLPSPTGE
     SNELQLHGRG VFVCISPWNF PLAIFLGQVA AALAAGNSVI AKPAEQTNLI GYYAVKLLHD
     AGVPADVVQY LPGDGATVGA ALTADPRVAG VAFTGSTDTA RAINRAMAAR DAAIGVLIAE
     TGGQNAFIAD SSALPEQLVK DAIGSAFTSA GQRCSAARVL FVQDDIADKV MTMLAGAMKE
     LKVGNPGLLS TDVGPVIDAD ALKILQDHAE RMDREARLIA AAELSVEAAN GTFFAPRAYE
     LKDLGQLQKE VFGPVLHVIR WKGDQLDAVI DQINATGYGL TLGVHSRIDE TVDRISNGVH
     VGNVYVNRNQ IGAVVGVQPF GGQGLSGTGP KAGGPHYLLR FATEKTVTVN TTAAGGNASL
     LTLGD
//

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