ARGD_AQUAE
ID ARGD_AQUAE Reviewed; 376 AA.
AC O66442;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
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=aq_023;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-376 IN COMPLEX WITH PLP.
RC STRAIN=VF5;
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of acetylornithine aminotransferase from Aquifex
RT aeolicus vf5.";
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}.
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; AE000657; AAC06390.1; -; Genomic_DNA.
DR PIR; G70301; G70301.
DR RefSeq; NP_213001.1; NC_000918.1.
DR RefSeq; WP_010879939.1; NC_000918.1.
DR PDB; 2EH6; X-ray; 1.90 A; A/B=2-376.
DR PDBsum; 2EH6; -.
DR AlphaFoldDB; O66442; -.
DR SMR; O66442; -.
DR STRING; 224324.aq_023; -.
DR EnsemblBacteria; AAC06390; AAC06390; aq_023.
DR KEGG; aae:aq_023; -.
DR PATRIC; fig|224324.8.peg.16; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_0; -.
DR InParanoid; O66442; -.
DR OMA; GMTTQIY; -.
DR OrthoDB; 572533at2; -.
DR UniPathway; UPA00068; UER00109.
DR EvolutionaryTrace; O66442; -.
DR Proteomes; UP000000798; 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..376
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112715"
FT BINDING 96..97
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000269|Ref.2"
FT BINDING 128
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000305|Ref.2"
FT BINDING 131
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 213..216
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000305|Ref.2"
FT BINDING 270
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 271
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000269|Ref.2"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107,
FT ECO:0000269|Ref.2"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2EH6"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2EH6"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:2EH6"
FT TURN 215..222
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 276..309
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2EH6"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:2EH6"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:2EH6"
FT HELIX 362..375
FT /evidence="ECO:0007829|PDB:2EH6"
SQ SEQUENCE 376 AA; 42009 MW; D4A963D54634030A CRC64;
MTYLMNNYAR LPVKFVRGKG VYLYDEEGKE YLDFVSGIGV NSLGHAYPKL TEALKEQVEK
LLHVSNLYEN PWQEELAHKL VKHFWTEGKV FFANSGTESV EAAIKLARKY WRDKGKNKWK
FISFENSFHG RTYGSLSATG QPKFHKGFEP LVPGFSYAKL NDIDSVYKLL DEETAGIIIE
VIQGEGGVNE ASEDFLSKLQ EICKEKDVLL IIDEVQTGIG RTGEFYAYQH FNLKPDVIAL
AKGLGGGVPI GAILAREEVA QSFTPGSHGS TFGGNPLACR AGTVVVDEVE KLLPHVREVG
NYFKEKLKEL GKGKVKGRGL MLGLELEREC KDYVLKALEK GLLINCTAGK VLRFLPPLII
QKEHIDRAIS VLREIL
