ARGD_ECOLI
ID ARGD_ECOLI Reviewed; 406 AA.
AC P18335; Q2M725;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305};
DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000303|PubMed:2199330};
DE Short=DapATase {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000303|PubMed:10074354};
DE Short=Succinyldiaminopimelate transferase {ECO:0000255|HAMAP-Rule:MF_01107};
DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:10074354};
DE EC=2.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:10074354};
GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107};
GN Synonyms=dapC {ECO:0000255|HAMAP-Rule:MF_01107}, dtu;
GN OrderedLocusNames=b3359, JW3322;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2199330; DOI=10.1016/0378-1119(90)90440-3;
RA Heimberg H., Boyen A., Crabeel M., Glansdorff N.;
RT "Escherichia coli and Saccharomyces cerevisiae acetylornithine
RT aminotransferase: evolutionary relationship with ornithine
RT aminotransferase.";
RL Gene 90:69-78(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP PROTEIN SEQUENCE OF 2-27 AND 69-77, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND PATHWAY.
RX PubMed=10074354; DOI=10.1021/bi982574a;
RA Ledwidge R., Blanchard J.S.;
RT "The dual biosynthetic capability of N-acetylornithine aminotransferase in
RT arginine and lysine biosynthesis.";
RL Biochemistry 38:3019-3024(1999).
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways. {ECO:0000255|HAMAP-Rule:MF_01107,
CC ECO:0000269|PubMed:10074354}.
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, ECO:0000269|PubMed:10074354};
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 ECO:0000269|PubMed:10074354};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107,
CC ECO:0000305|PubMed:10074354};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01107, ECO:0000305|PubMed:10074354};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for N-acetylornithine {ECO:0000269|PubMed:10074354};
CC KM=0.075 mM for N-succinyldiaminopimelate
CC {ECO:0000269|PubMed:10074354};
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, ECO:0000305|PubMed:10074354}.
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 ECO:0000305|PubMed:10074354}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107,
CC ECO:0000305}.
CC -!- MISCELLANEOUS: The reaction catalyzed by ACOAT is highly reversible.
CC This enzyme may also transaminate ornithine.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01107, ECO:0000305}.
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DR EMBL; M32796; AAA23480.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58156.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76384.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77931.1; -; Genomic_DNA.
DR PIR; B65130; B65130.
DR RefSeq; NP_417818.1; NC_000913.3.
DR RefSeq; WP_000963792.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P18335; -.
DR SMR; P18335; -.
DR BioGRID; 4260742; 7.
DR DIP; DIP-9138N; -.
DR IntAct; P18335; 6.
DR STRING; 511145.b3359; -.
DR SWISS-2DPAGE; P18335; -.
DR jPOST; P18335; -.
DR PaxDb; P18335; -.
DR PRIDE; P18335; -.
DR EnsemblBacteria; AAC76384; AAC76384; b3359.
DR EnsemblBacteria; BAE77931; BAE77931; BAE77931.
DR GeneID; 58460184; -.
DR GeneID; 947864; -.
DR KEGG; ecj:JW3322; -.
DR KEGG; eco:b3359; -.
DR PATRIC; fig|1411691.4.peg.3371; -.
DR EchoBASE; EB0064; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_6; -.
DR InParanoid; P18335; -.
DR OMA; MVPNYNP; -.
DR PhylomeDB; P18335; -.
DR BioCyc; EcoCyc:ACETYLORNTRANSAM-MON; -.
DR BioCyc; MetaCyc:ACETYLORNTRANSAM-MON; -.
DR UniPathway; UPA00034; UER00020.
DR UniPathway; UPA00068; UER00109.
DR PRO; PR:P18335; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IDA:EcoliWiki.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0009016; F:succinyldiaminopimelate transaminase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Cytoplasm; Direct protein sequencing; Lysine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10074354,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..406
FT /note="Acetylornithine/succinyldiaminopimelate
FT aminotransferase"
FT /id="PRO_0000112743"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP-
FT Rule:MF_01107"
FT BINDING 141
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP-
FT Rule:MF_01107"
FT BINDING 144
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5, ECO:0000255|HAMAP-
FT Rule:MF_01107"
FT BINDING 226..229
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP-
FT Rule:MF_01107"
FT BINDING 283
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000250|UniProtKB:Q5SHH5, ECO:0000255|HAMAP-
FT Rule:MF_01107"
FT BINDING 284
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP-
FT Rule:MF_01107"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P40732, ECO:0000255|HAMAP-
FT Rule:MF_01107"
FT CONFLICT 245..247
FT /note="GVT -> ALA (in Ref. 1; AAA23480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 43767 MW; 645AA1EBCA442214 CRC64;
MAIEQTAITR ATFDEVILPI YAPAEFIPVK GQGSRIWDQQ GKEYVDFAGG IAVTALGHCH
PALVNALKTQ GETLWHISNV FTNEPALRLG RKLIEATFAE RVVFMNSGTE ANETAFKLAR
HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPADIIH VPFNDLHAVK
AVMDDHTCAV VVEPIQGEGG VTAATPEFLQ GLRELCDQHQ ALLVFDEVQC GMGRTGDLFA
YMHYGVTPDI LTSAKALGGG FPISAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD
IINTPEVLEG IQAKRQRFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY KGRARDFLYA
GAEAGVMVLN AGPDVMRFAP SLVVEDADID EGMQRFAHAV AKVVGA
