ARGD_CAMJE
ID ARGD_CAMJE Reviewed; 393 AA.
AC Q9PIR7; Q0PBS7; Q9RGZ7;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
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=Cj0227;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=10588044; DOI=10.1139/w99-095;
RA Hani E.K., Ng D., Chan V.-L.;
RT "Arginine biosynthesis in Campylobacter jejuni TGH9011: determination of
RT the argCOBD cluster.";
RL Can. J. Microbiol. 45:959-969(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF21805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAL34382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL111168; CAL34382.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF093219; AAF21805.1; ALT_INIT; Genomic_DNA.
DR PIR; C81440; C81440.
DR RefSeq; YP_002343670.1; NC_002163.1.
DR PDB; 3NX3; X-ray; 1.80 A; A/B=1-393.
DR PDBsum; 3NX3; -.
DR AlphaFoldDB; Q9PIR7; -.
DR SMR; Q9PIR7; -.
DR IntAct; Q9PIR7; 12.
DR STRING; 192222.Cj0227; -.
DR PaxDb; Q9PIR7; -.
DR PRIDE; Q9PIR7; -.
DR EnsemblBacteria; CAL34382; CAL34382; Cj0227.
DR GeneID; 904555; -.
DR KEGG; cje:Cj0227; -.
DR PATRIC; fig|192222.6.peg.221; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_7; -.
DR OMA; KYSSDYA; -.
DR UniPathway; UPA00068; UER00109.
DR EvolutionaryTrace; Q9PIR7; -.
DR Proteomes; UP000000799; 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: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..393
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112736"
FT BINDING 100..101
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 132
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 135
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 217..220
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 275
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 276
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT MOD_RES 246
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT CONFLICT 10..12
FT /note="IPT -> VPA (in Ref. 1; AAF21805)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="V -> I (in Ref. 1; AAF21805)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="S -> N (in Ref. 1; AAF21805)"
FT /evidence="ECO:0000305"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3NX3"
FT TURN 219..226
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3NX3"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 281..296
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 299..320
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3NX3"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3NX3"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:3NX3"
FT HELIX 376..391
FT /evidence="ECO:0007829|PDB:3NX3"
SQ SEQUENCE 393 AA; 43519 MW; 62AE74E1696FFC55 CRC64;
MDYKEQSHII PTYKRFDIVL EKGQGVYLFD DKAKKYLDFS SGIGVCALGY NHAKFNAKIK
AQVDKLLHTS NLYYNENIAA AAKNLAKASA LERVFFTNSG TESIEGAMKT ARKYAFNKGV
KGGQFIAFKH SFHGRTLGAL SLTANEKYQK PFKPLISGVK FAKYNDISSV EKLVNEKTCA
IILESVQGEG GINPANKDFY KALRKLCDEK DILLIADEIQ CGMGRSGKFF AYEHAQILPD
IMTSAKALGC GLSVGAFVIN QKVASNSLEA GDHGSTYGGN PLVCAGVNAV FEIFKEEKIL
ENVNKLTPYL EQSLDELINE FDFCKKRKGL GFMQGLSLDK SVKVAKVIQK CQENALLLIS
CGENDLRFLP PLILQKEHID EMSEKLRKAL KSF
