ARGD_THEMA
ID ARGD_THEMA Reviewed; 385 AA.
AC Q9X2A5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Acetylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107};
DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107};
DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107};
GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; OrderedLocusNames=TM_1785;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH PLP.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of acetylornithine aminotransferase from Thermotoga
RT maritima.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PLP.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11)
RT (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
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 -!- 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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107,
CC ECO:0000305|Ref.2, ECO:0000305|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}.
CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate aminotransferase
CC activity, thus carrying out the corresponding step in lysine
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01107}.
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; AE000512; AAD36848.1; -; Genomic_DNA.
DR PIR; D72211; D72211.
DR RefSeq; NP_229582.1; NC_000853.1.
DR RefSeq; WP_004082331.1; NZ_CP011107.1.
DR PDB; 2E54; X-ray; 1.50 A; A=1-385.
DR PDB; 2ORD; X-ray; 1.40 A; A/B=1-385.
DR PDBsum; 2E54; -.
DR PDBsum; 2ORD; -.
DR AlphaFoldDB; Q9X2A5; -.
DR SMR; Q9X2A5; -.
DR STRING; 243274.THEMA_05275; -.
DR EnsemblBacteria; AAD36848; AAD36848; TM_1785.
DR KEGG; tma:TM1785; -.
DR eggNOG; COG4992; Bacteria.
DR InParanoid; Q9X2A5; -.
DR OMA; FWGWQAH; -.
DR OrthoDB; 572533at2; -.
DR UniPathway; UPA00068; UER00109.
DR EvolutionaryTrace; Q9X2A5; -.
DR Proteomes; UP000008183; 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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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; 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; 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; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..385
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112805"
FT BINDING 94..95
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT BINDING 126
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000305|Ref.2, ECO:0000305|Ref.3"
FT BINDING 129
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 211..214
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000305|Ref.2, ECO:0000305|Ref.3"
FT BINDING 267
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 268
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000269|Ref.3"
FT MOD_RES 240
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:2ORD"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 94..112
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2ORD"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2ORD"
FT TURN 213..220
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:2ORD"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2E54"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 291..312
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:2ORD"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2ORD"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:2ORD"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:2ORD"
SQ SEQUENCE 385 AA; 42884 MW; 4018F87FCBEBFFE0 CRC64;
MYLMNTYSRF PATFVYGKGS WIYDEKGNAY LDFTSGIAVN VLGHSHPRLV EAIKDQAEKL
IHCSNLFWNR PQMELAELLS KNTFGGKVFF ANTGTEANEA AIKIARKYGK KKSEKKYRIL
SAHNSFHGRT LGSLTATGQP KYQKPFEPLV PGFEYFEFNN VEDLRRKMSE DVCAVFLEPI
QGESGIVPAT KEFLEEARKL CDEYDALLVF DEVQCGMGRT GKLFAYQKYG VVPDVLTTAK
GLGGGVPIGA VIVNERANVL EPGDHGTTFG GNPLACRAGV TVIKELTKEG FLEEVEEKGN
YLMKKLQEMK EEYDVVADVR GMGLMIGIQF REEVSNREVA TKCFENKLLV VPAGNNTIRF
LPPLTVEYGE IDLAVETLKK VLQGI
