ARGD_SALTY
ID ARGD_SALTY Reviewed; 405 AA.
AC P40732;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Acetylornithine/succinyldiaminopimelate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305};
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, ECO:0000269|PubMed:17680699};
DE EC=2.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01107};
GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; Synonyms=dapC, dtu;
GN OrderedLocusNames=STM3468;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=2403545; DOI=10.1128/jb.172.1.397-410.1990;
RA Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.;
RT "Chromosomal organization and expression of Escherichia coli pabA.";
RL J. Bacteriol. 172:397-410(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEXES WITH PLP, CATALYTIC
RP ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=17680699; DOI=10.1002/prot.21567;
RA Rajaram V., Ratna Prasuna P., Savithri H.S., Murthy M.R.;
RT "Structure of biosynthetic N-acetylornithine aminotransferase from
RT Salmonella typhimurium: studies on substrate specificity and inhibitor
RT binding.";
RL Proteins 70:429-441(2008).
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, ECO:0000269|PubMed:17680699};
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 ECO:0000269|PubMed:17680699};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01107, ECO:0000269|PubMed:17680699};
CC -!- ACTIVITY REGULATION: Inhibited by gabaculine (Gcn).
CC {ECO:0000269|PubMed:17680699}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for N-acetylornithine (at pH 9.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17680699};
CC KM=640 uM for ornithine (at pH 9.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17680699};
CC pH dependence:
CC Optimum pH is 9.5. At pH 8.0, the activity is reduced by 50%.
CC {ECO:0000269|PubMed:17680699};
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:17680699}.
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 ECO:0000269|PubMed:17680699}.
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.
CC {ECO:0000269|PubMed:17680699}.
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; AE006468; AAL22330.1; -; Genomic_DNA.
DR EMBL; M32354; AAA24265.1; -; Genomic_DNA.
DR EMBL; M32355; AAA27178.1; -; Genomic_DNA.
DR RefSeq; NP_462371.1; NC_003197.2.
DR RefSeq; WP_000190023.1; NC_003197.2.
DR PDB; 2PB0; X-ray; 1.96 A; A/B=1-405.
DR PDB; 2PB2; X-ray; 1.91 A; A/B=1-405.
DR PDB; 4JEV; X-ray; 1.67 A; A/B=1-405.
DR PDB; 4JEW; X-ray; 1.48 A; A/B=1-405.
DR PDB; 4JEX; X-ray; 1.43 A; A/B=1-405.
DR PDB; 4JEY; X-ray; 1.55 A; A/B=1-405.
DR PDB; 4JEZ; X-ray; 1.55 A; A/B=1-405.
DR PDB; 4JF0; X-ray; 2.10 A; A/B=1-405.
DR PDB; 4JF1; X-ray; 1.28 A; A/B=1-405.
DR PDBsum; 2PB0; -.
DR PDBsum; 2PB2; -.
DR PDBsum; 4JEV; -.
DR PDBsum; 4JEW; -.
DR PDBsum; 4JEX; -.
DR PDBsum; 4JEY; -.
DR PDBsum; 4JEZ; -.
DR PDBsum; 4JF0; -.
DR PDBsum; 4JF1; -.
DR AlphaFoldDB; P40732; -.
DR SMR; P40732; -.
DR STRING; 99287.STM3468; -.
DR PaxDb; P40732; -.
DR EnsemblBacteria; AAL22330; AAL22330; STM3468.
DR GeneID; 1254991; -.
DR KEGG; stm:STM3468; -.
DR PATRIC; fig|99287.12.peg.3665; -.
DR HOGENOM; CLU_016922_10_1_6; -.
DR OMA; MVPNYNP; -.
DR PhylomeDB; P40732; -.
DR BioCyc; SENT99287:STM3468-MON; -.
DR SABIO-RK; P40732; -.
DR UniPathway; UPA00034; UER00020.
DR UniPathway; UPA00068; UER00109.
DR EvolutionaryTrace; P40732; -.
DR Proteomes; UP000001014; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Arginine biosynthesis; Cytoplasm; Lysine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..405
FT /note="Acetylornithine/succinyldiaminopimelate
FT aminotransferase"
FT /id="PRO_0000112777"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000269|PubMed:17680699"
FT BINDING 141
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000305|PubMed:17680699"
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 ECO:0000305|PubMed:17680699"
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 ECO:0000269|PubMed:17680699"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000269|PubMed:17680699"
FT CONFLICT 3
FT /note="T -> I (in Ref. 2; AAA24265/AAA27178)"
FT /evidence="ECO:0000305"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4JF1"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4JF1"
FT TURN 228..235
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4JEX"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 305..329
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:4JF1"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:4JF1"
FT HELIX 386..405
FT /evidence="ECO:0007829|PDB:4JF1"
SQ SEQUENCE 405 AA; 43670 MW; 26A69C62831E986C CRC64;
MATEQTAITR ATFDEVILPV YAPADFIPVK GKGSRVWDQQ GKEYIDFAGG IAVTALGHCH
PALVEALKSQ GETLWHTSNV FTNEPALRLG RKLIDATFAE RVLFMNSGTE ANETAFKLAR
HYACVRHSPF KTKIIAFHNA FHGRSLFTVS VGGQPKYSDG FGPKPADIIH VPFNDLHAVK
AVMDDHTCAV VVEPIQGEGG VQAATPEFLK GLRDLCDEHQ ALLVFDEVQC GMGRTGDLFA
YMHYGVTPDI LTSAKALGGG FPVSAMLTTQ EIASAFHVGS HGSTYGGNPL ACAVAGAAFD
IINTPEVLQG IHTKRQQFVQ HLQAIDEQFD IFSDIRGMGL LIGAELKPKY KGRARDFLYA
GAEAGVMVLN AGADVMRFAP SLVVEEADIH EGMQRFAQAV GKVVA
