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PROA_BACSU
ID   PROA_BACSU              Reviewed;         415 AA.
AC   P39821; O35032;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GPR {ECO:0000255|HAMAP-Rule:MF_00412};
DE            EC=1.2.1.41 {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE   AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
DE            Short=GSA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00412};
GN   Name=proA {ECO:0000255|HAMAP-Rule:MF_00412}; OrderedLocusNames=BSU13130;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8083159; DOI=10.1128/jb.176.18.5673-5680.1994;
RA   Ogura M., Kawata-Mukai M., Itaya M., Takio K., Tanaka T.;
RT   "Multiple copies of the proB gene enhance degS-dependent extracellular
RT   protease production in Bacillus subtilis.";
RL   J. Bacteriol. 176:5673-5680(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Devine K.M.;
RT   "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 359.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-
CC       phosphate into L-glutamate 5-semialdehyde and phosphate. The product
CC       spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
CC       {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC         glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00412};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyl phosphate reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00412}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05045.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D26044; BAA05045.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AJ002571; CAA05592.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13170.2; -; Genomic_DNA.
DR   PIR; C69682; C69682.
DR   RefSeq; NP_389196.2; NC_000964.3.
DR   RefSeq; WP_003245312.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P39821; -.
DR   SMR; P39821; -.
DR   STRING; 224308.BSU13130; -.
DR   jPOST; P39821; -.
DR   PaxDb; P39821; -.
DR   PRIDE; P39821; -.
DR   EnsemblBacteria; CAB13170; CAB13170; BSU_13130.
DR   GeneID; 936166; -.
DR   KEGG; bsu:BSU13130; -.
DR   PATRIC; fig|224308.179.peg.1425; -.
DR   eggNOG; COG0014; Bacteria.
DR   InParanoid; P39821; -.
DR   OMA; PGVCNAM; -.
DR   PhylomeDB; P39821; -.
DR   BioCyc; BSUB:BSU13130-MON; -.
DR   UniPathway; UPA00098; UER00360.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_00412; ProA; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR012134; Glu-5-SA_DH.
DR   InterPro; IPR000965; GPR_dom.
DR   Pfam; PF00171; Aldedh; 2.
DR   PIRSF; PIRSF000151; GPR; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR00407; proA; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   CHAIN           1..415
FT                   /note="Gamma-glutamyl phosphate reductase"
FT                   /id="PRO_0000189696"
FT   CONFLICT        108
FT                   /note="E -> Q (in Ref. 1; BAA05045)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="A -> T (in Ref. 1; BAA05045)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="H -> N (in Ref. 1; BAA05045)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="A -> R (in Ref. 2; CAA05592)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   415 AA;  45252 MW;  9FB7B0C04C9F62D0 CRC64;
     MSEVSVKAKL AKEAAAEMIM KTTAEKDEAL SLIANGLRKE LDFLLAENAK DIVNGKENGL
     TPDIIDRLSL DEKRIRDIAD AVELLIDLAD PIGDSLETIE KENGLFIEKI RVPLGVVGMI
     YEARPNVTVD AATLCLKTGN AVVLRGSSSA IHSNKALVSV IYRALEQSAL PIHAVQLIED
     TSRETAKELF TLNDGLDVLI PRGGKKLIDL VVRESTVPVL ETGAGNCHIF IDETAKPQMA
     EKVVVNAKTQ RPSVCNAIES LLIHKAWARQ HGKELLDQLE NAGVEIRGDE LVCELHPSSK
     QASKEDWETE FLAPVLSVKT VENVQEAVKH IQQYGTNHSE AILTENDKNA VYFQTAVDAA
     AVYHNASTRF TDGFEFGYGA EIGISTQKLH ARGPMGLPAL TSTKYIIKGT GQIRE
 
 
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