ID ARGD_SULTO Reviewed; 387 AA.
AC Q976K0; F9VMN6;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 01-MAY-2013, entry version 85.
DE RecName: Full=Acetylornithine/acetyl-lysine aminotransferase;
DE Short=ACOAT;
DE EC=2.6.1.-;
DE EC=2.6.1.11;
GN Name=argD; Synonyms=lysJ; OrderedLocusNames=STK_01910;
OS Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M.,
RA Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S.,
RA Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y.,
RA Yoshizawa T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T.,
RA Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic
RT Crenarchaeon, Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Involved in both the arginine and lysine biosynthetic
CC pathways (By similarity).
CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-
CC acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-lysine + 2-oxoglutarate = N-
CC acetyl-L-aminoadipate semialdehyde + L-glutamate.
CC -!- COFACTOR: Binds 1 pyridoxal phosphate per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC acetyl-L-ornithine from L-glutamate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step
CC 4/5.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. ArgD subfamily.
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DR EMBL; BA000023; BAK54182.1; -; Genomic_DNA.
DR RefSeq; NP_376038.1; NC_003106.2.
DR ProteinModelPortal; Q976K0; -.
DR STRING; 273063.ST0191; -.
DR EnsemblBacteria; BAK54182; BAK54182; STK_01910.
DR GeneID; 1458075; -.
DR KEGG; sto:ST0191; -.
DR eggNOG; COG4992; -.
DR HOGENOM; HOG000020206; -.
DR KO; K05830; -.
DR OMA; EPDIFTA; -.
DR ProtClustDB; CLSK883609; -.
DR UniPathway; UPA00033; UER00038.
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:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01107; ArgD_aminotrans_3; 1; -.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR InterPro; IPR004636; Trfase_AcOrn/SuccOrn_fam.
DR PANTHER; PTHR11986; PTHR11986; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 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 Complete proteome; Cytoplasm; Lysine biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1 387 Acetylornithine/acetyl-lysine
FT aminotransferase.
FT /FTId=PRO_0000112831.
FT REGION 96 97 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 207 210 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 123 123 Pyridoxal phosphate; via carbonyl oxygen
FT (By similarity).
FT BINDING 126 126 N2-acetyl-L-ornithine (By similarity).
FT BINDING 264 264 N2-acetyl-L-ornithine (By similarity).
FT BINDING 265 265 Pyridoxal phosphate (By similarity).
FT MOD_RES 236 236 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 387 AA; 42935 MW; 7BF625CA4EAE6F9E CRC64;
MKFIQLYGDR GLTIVKGEGQ YVWDISGTKY LDLHTGIGVA FLGHRNRRVI EYLSRQMENI
MTLSTSFSTP IRDEMLKELD PLKPDKMDNI ILLNSGTEAV EAALKTARKI TGRKKIIAFK
NSFHGRTAGS LSVTWNKRYR EPFEPLMSPV QFLTYNNIDE LKNIDEQTAA VIVEPIQGES
GVIPANEDFM KALREQTQKV GALLVVDEVQ TGFGRTGKVW AYQHYGIIPD LLTAGKAIGG
GFPVSALFLP DWIAEKLEEG DHGSTYGGNP MAMAAVTAAS KVLKEDNVVE QASIKGEIFK
KILREKLSDL KSVREIRGKG LMIGIEIRFP PAIALKVMQD ERVLALKAGS TVIRFLAPYM
ITQSDMEEAS NAARKGIIET ENKRAIT
//
