ARGD_STRMU
ID ARGD_STRMU Reviewed; 379 AA.
AC Q59928;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
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=SMU_666;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JH1005;
RX PubMed=8763945; DOI=10.1128/jb.178.14.4166-4175.1996;
RA Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P.,
RA Bleiweis A.S.;
RT "Insertional mutagenesis and recovery of interrupted genes of Streptococcus
RT mutans by using transposon Tn917: preliminary characterization of mutants
RT displaying acid sensitivity and nutritional requirements.";
RL J. Bacteriol. 178:4166-4175(1996).
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; AE014133; AAN58400.1; -; Genomic_DNA.
DR EMBL; U48887; AAC44504.1; -; Genomic_DNA.
DR RefSeq; NP_721094.1; NC_004350.2.
DR RefSeq; WP_002261875.1; NC_004350.2.
DR AlphaFoldDB; Q59928; -.
DR SMR; Q59928; -.
DR STRING; 210007.SMU_666; -.
DR PRIDE; Q59928; -.
DR EnsemblBacteria; AAN58400; AAN58400; SMU_666.
DR KEGG; smu:SMU_666; -.
DR PATRIC; fig|210007.7.peg.591; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_9; -.
DR OMA; PFMVPTY; -.
DR PhylomeDB; Q59928; -.
DR UniPathway; UPA00068; UER00109.
DR Proteomes; UP000002512; 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..379
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112801"
FT BINDING 93..94
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 120
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 123
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 205..208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 262
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 263
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT CONFLICT 148
FT /note="H -> N (in Ref. 2; AAC44504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 41142 MW; 84CA88267A4C770A CRC64;
MSNLFQNYTR ADLEFIKAEG NYLFDTQGKK YLDFSTGIGV TNLGFHPQVQ VALQKQAEQI
WHTPNLYQNS LQEEVAAKLM AGKDYLAFFC NSGAEANEAA IKIARKATGK QEIITFQNSF
HGRTFGSMSA TGQDKIKVGF GDAVPHFHYA VFNDLNSVKA LVTENTAAVM LELVQGESGV
LPAEQDFVTA LADYCQKNGL LLIIDEVQTG MGRTGKLYAF QHYGIEPDIF TLAKGLANGV
PVGAMLAKKQ FGSAFGPGSH GSTFGGNKLA MAASSAVLDI MTKAGFLEQA WENAHYLQEQ
LTSALQVADT VTQVRGLGYM IGIETTADLG QLVKATRDRG LIVLTAGTNV IRLLPPLTLT
KDEIDQGIMI LQEVFEQHN
