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ARGD_ECO57
ID   ARGD_ECO57              Reviewed;         406 AA.
AC   Q8X4S6;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107};
DE            Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107};
DE            Short=DapATase {ECO:0000255|HAMAP-Rule:MF_01107};
DE            Short=Succinyldiaminopimelate transferase {ECO:0000255|HAMAP-Rule:MF_01107};
DE            EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107};
DE            EC=2.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01107};
GN   Name=argD {ECO:0000255|HAMAP-Rule:MF_01107};
GN   Synonyms=dapC {ECO:0000255|HAMAP-Rule:MF_01107};
GN   OrderedLocusNames=Z4720, ECs4210;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC       pathways. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC         acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01107};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC         (S)-2-succinylamino-6-oxoheptanedioate + L-glutamate;
CC         Xref=Rhea:RHEA:11960, ChEBI:CHEBI:15685, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58087; EC=2.6.1.17;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01107};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01107};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01107};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01107}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 2/3. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}.
CC   -!- MISCELLANEOUS: The reaction catalyzed by ACOAT is highly reversible.
CC       This enzyme may also transaminate ornithine (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01107}.
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DR   EMBL; AE005174; AAG58467.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37633.1; -; Genomic_DNA.
DR   PIR; B91155; B91155.
DR   PIR; G86000; G86000.
DR   RefSeq; NP_312237.1; NC_002695.1.
DR   RefSeq; WP_000963819.1; NZ_SEKU01000003.1.
DR   AlphaFoldDB; Q8X4S6; -.
DR   SMR; Q8X4S6; -.
DR   STRING; 155864.EDL933_4563; -.
DR   PRIDE; Q8X4S6; -.
DR   EnsemblBacteria; AAG58467; AAG58467; Z4720.
DR   EnsemblBacteria; BAB37633; BAB37633; ECs_4210.
DR   GeneID; 915934; -.
DR   KEGG; ece:Z4720; -.
DR   KEGG; ecs:ECs_4210; -.
DR   PATRIC; fig|386585.9.peg.4394; -.
DR   eggNOG; COG4992; Bacteria.
DR   HOGENOM; CLU_016922_10_1_6; -.
DR   OMA; MVPNYNP; -.
DR   UniPathway; UPA00034; UER00020.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR017652; Ac/SucOrn_transaminase_bac.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03246; arg_catab_astC; 1.
DR   TIGRFAMs; TIGR00707; argD; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW   Cytoplasm; Lysine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..406
FT                   /note="Acetylornithine/succinyldiaminopimelate
FT                   aminotransferase"
FT                   /id="PRO_0000112745"
FT   BINDING         108..109
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         141
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         144
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         226..229
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         283
FT                   /ligand="N(2)-acetyl-L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:57805"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   BINDING         284
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT   MOD_RES         255
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
SQ   SEQUENCE   406 AA;  43755 MW;  90C65E1438466979 CRC64;
     MAIEQTAITR ATFDEVILPI YAPAEFIPVK GQGSRIWDQQ GKEYVDFAGG IAVTALGHCH
     PALVNALKTQ GETLWHISNV FTNEPALRLG RKLIEATFAE RVVFMNSGTE ANETAFKLAR
     HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPSDIIH VPFNDLHAVK
     AVMDDHTCAV VVEPIQGEGG VTAATPEFLQ GLRELCDQHQ ALLVFDEVQC GMGRTGDLFA
     YMHYGVTPDI LTSAKALGGG FPISAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD
     IINTPEVLEG IQAKRQRFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY KGQARDFLYA
     GAEAGVMVLN AGPDVMRFAP SLVVEDADID EGMQRFAHAV AKVVGA
 
 
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