ARGD_GEOSE
ID ARGD_GEOSE Reviewed; 385 AA.
AC Q07907; Q9ZB64;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 116.
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};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149.
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=8473852; DOI=10.1099/00221287-139-3-393;
RA Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I.,
RA Pierard P., Glansdorff N.;
RT "Primary structure, partial purification and regulation of key enzymes of
RT the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus:
RT dual function of ornithine acetyltransferase.";
RL J. Gen. Microbiol. 139:393-402(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 148-385.
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
RX PubMed=9370352; DOI=10.1111/j.1432-1033.1997.00443.x;
RA Yang H., Park S.M., Nolan W.G., Lu C.-D., Abdelal A.T.;
RT "Cloning and characterization of the arginine-specific carbamoyl-phosphate
RT synthetase from Bacillus stearothermophilus.";
RL Eur. J. Biochem. 249:443-449(1997).
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; L06036; AAA22199.1; -; Genomic_DNA.
DR EMBL; U43091; AAC78718.1; -; Genomic_DNA.
DR PIR; I39768; I39768.
DR AlphaFoldDB; Q07907; -.
DR SMR; Q07907; -.
DR UniPathway; UPA00068; UER00109.
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; Transferase.
FT CHAIN 1..385
FT /note="Acetylornithine aminotransferase"
FT /id="PRO_0000112720"
FT BINDING 95..96
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 122
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 125
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 207..210
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 264
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01107"
SQ SEQUENCE 385 AA; 41304 MW; A40E6AC2ED105604 CRC64;
MSALFPTYNR WNIAVQSAEG TVVTDVNGKQ YLDFVSGIAV CNLGHRHPHV QKSIEQQLNQ
YWHVSNLFTI PIQEEVASLL VAHSAGDYVF FCNSGAEANE AALKLARKHT GRHKVITFRQ
SFHGRTFATM AATGQEKVHS GFGPLLPEFI HLPLNDVDAL KQAMSEEVAA VMLEVVQGEG
GVRPVDPAFL QTASELCQQH GALLIIDEVQ TGIGRTGKPF AYQHFDVEPD IITAAKGLGS
GIPVGAMIGK AFLKESFGPG VHGSTFGGNP IAMAAAKATL EVVFDPAFLQ DVQEKGRYFL
ARLHDALASL DIVKDVRGLG LLVGIECQTD VAPLLPLIHE NGLLVLSAGP NVIRLLPLVV
TKAEIDEAVD ILTNVLNNAN ASAVL
