ARGD_PSEPK
ID ARGD_PSEPK Reviewed; 406 AA.
AC P59319;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=PP_4481;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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}.
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DR EMBL; AE015451; AAN70056.1; -; Genomic_DNA.
DR RefSeq; NP_746592.1; NC_002947.4.
DR RefSeq; WP_010955178.1; NC_002947.4.
DR AlphaFoldDB; P59319; -.
DR SMR; P59319; -.
DR STRING; 160488.PP_4481; -.
DR EnsemblBacteria; AAN70056; AAN70056; PP_4481.
DR KEGG; ppu:PP_4481; -.
DR PATRIC; fig|160488.4.peg.4767; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_6; -.
DR OMA; PFMVPTY; -.
DR PhylomeDB; P59319; -.
DR BioCyc; PPUT160488:G1G01-4782-MON; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000000556; 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; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112769"
FT BINDING 108..109
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 141
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
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 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 MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
SQ SEQUENCE 406 AA; 43490 MW; 5597D2F10C3E221E CRC64;
MSVEQAPVQR ADFDQVMVPN YSPAAFIPVR GEGSRVWDQS GRELIDFAGG IAVNALGHCH
PALVKALTEQ ANTLWHVSNV FTNEPALRLA HKLVDATFAD RAFFCNSGAE SNEAAFKLAR
RVAHDRFGPQ KHEIIATVNS FHGRTLFTVS VGGQPKYSDG FGPKITGISH VPYNDLEALK
AQISDKTCAV VIEPIQGESG VVPADKAYLE GARKLCDEHN ALLIFDEVQT GVGRTGSLYA
YQHYGVIPDI LTSAKSLGGG FPIGAMLTTT ELAKHLAVGT HGTTYGGNPL GCAVACAVLD
VVNTPETLAG IKAKHERFKT RLEQIGQQYN LFSQVRGVGL LLGCVLTEAW KGKAKDVLNA
AEKEGVMVLQ AGPDVVRFAP SLVVEDADID EGLDRFERAV ATLTKG
