ARGD_CORGL
ID ARGD_CORGL Reviewed; 391 AA.
AC Q59282;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
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};
GN OrderedLocusNames=Cgl1397, cg1583;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=8581175; DOI=10.1099/13500872-142-1-99;
RA Sakanyan V., Petrosyan P., Lecocq M., Boyen A., Legrain C., Demarez M.N.,
RA Hallet J.-N., Glansdorff N.;
RT "Genes and enzymes of the acetyl cycle of arginine biosynthesis in
RT Corynebacterium glutamicum: enzyme evolution in the early steps of the
RT arginine pathway.";
RL Microbiology 142:99-108(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Park M.Y., Chun J.Y., Ko S.-Y., Lee M.-S.;
RT "Molecular cloning of the arginine biosynthetic genes from Corynebacterium
RT glutamicum.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; X86157; CAA60099.1; -; Genomic_DNA.
DR EMBL; AF049897; AAC24815.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98790.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21408.1; -; Genomic_DNA.
DR RefSeq; NP_600616.1; NC_003450.3.
DR RefSeq; WP_011014334.1; NC_006958.1.
DR AlphaFoldDB; Q59282; -.
DR SMR; Q59282; -.
DR STRING; 196627.cg1583; -.
DR KEGG; cgb:cg1583; -.
DR KEGG; cgl:Cgl1397; -.
DR PATRIC; fig|196627.13.peg.1366; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_11; -.
DR OMA; PFMVPTY; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000000582; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..391
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112741"
FT BINDING 110..111
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 136
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 139
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 224..227
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 281
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 282
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT CONFLICT 267..268
FT /note="TG -> L (in Ref. 1; CAA60099 and 2; AAC24815)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..313
FT /note="GE -> Q (in Ref. 1; CAA60099 and 2; AAC24815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 41206 MW; 10EF51CAC4FE1A1B CRC64;
MSTLETWPQV IINTYGTPPV ELVSGKGATV TDDQGNVYID LLAGIAVNAL GHAHPAIIEA
VTNQIGQLGH VSNLFASRPV VEVAEELIKR FSLDDATLAA QTRVFFCNSG AEANEAAFKI
ARLTGRSRIL AAVHGFHGRT MGSLALTGQP DKREAFLPMP SGVEFYPYGD TDYLRKMVET
NPTDVAAIFL EPIQGETGVV PAPEGFLKAV RELCDEYGIL MITDEVQTGV GRTGDFFAHQ
HDGVVPDVVT MAKGLGGGLP IGACLATGRA AELMTPGKHG TTFGGNPVAC AAAKAVLSVV
DDAFCAEVAR KGELFKELLA KVDGVVDVRG RGLMLGVVLE RDVAKQAVLD GFKHGVILNA
PADNIIRLTP PLVITDEEIA DAVKAIAETI A
