ID ARGD_BACAN Reviewed; 386 AA. AC Q81M98; Q6HTQ1; Q6KIZ6; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 16-JUN-2009, entry version 51. DE RecName: Full=Acetylornithine aminotransferase; DE Short=ACOAT; DE EC=2.6.1.11; GN Name=argD; OrderedLocusNames=BA_4352, GBAA_4352, BAS4037; OS Bacillus anthracis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames / isolate Porton; RX MEDLINE=22608414; PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., RA Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., RA Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., RA Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., RA Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., RA Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., RA Hanna P.C., Kolstoe A.-B., Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to RT closely related bacteria."; RL Nature 423:81-86(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor; RA Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., RA Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., RA Fraser C.M.; RT "Bacillus anthracis comparative genomics."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-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 -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate CC aminotransferase activity, thus carrying out the corresponding CC step in lysine biosynthesis. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016879; AAP28070.1; -; Genomic_DNA. DR EMBL; AE017334; AAT35422.1; -; Genomic_DNA. DR EMBL; AE017225; AAT56338.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_846584.1; -. DR RefSeq; YP_022688.1; -. DR RefSeq; YP_030287.2; -. DR HSSP; P12995; 1QJ3. DR GeneID; 1087573; -. DR GeneID; 2816449; -. DR GeneID; 2850294; -. DR GenomeReviews; AE016879_GR; BA_4352. DR GenomeReviews; AE017225_GR; BAS4037. DR GenomeReviews; AE017334_GR; GBAA4352. DR KEGG; ban:BA4352; -. DR KEGG; bar:GBAA4352; -. DR KEGG; bat:BAS4037; -. DR TIGR; BA_4352; -. DR TIGR; GBAA_4352; -. DR HOGENOM; Q81M98; -. DR OMA; Q81M98; DIWHISN. DR BioCyc; BANT260799:BAS4037-MON; -. DR BioCyc; BANT261594:GBAA4352-MON; -. DR BRENDA; 2.6.1.11; 267517. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-amin...; IEA:HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01107; -; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR004636; ArgD_aminotrans. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR PANTHER; PTHR11986; Aminotrans_3; 1. DR PANTHER; PTHR11986:SF19; ArgD_aminotrans; 1. DR Pfam; PF00202; Aminotran_3; 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; Pyridoxal phosphate; Transferase. FT CHAIN 1 386 Acetylornithine aminotransferase. FT /FTId=PRO_0000112716. FT REGION 208 211 Pyridoxal phosphate binding (By FT similarity). FT BINDING 123 123 Pyridoxal phosphate; via carbonyl oxygen FT (By similarity). FT BINDING 126 126 N(2)-acetyl-L-ornithine (By similarity). FT BINDING 265 265 N(2)-acetyl-L-ornithine (By similarity). FT BINDING 266 266 Pyridoxal phosphate (By similarity). FT MOD_RES 237 237 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 386 AA; 42179 MW; 24C581C59564DE0C CRC64; MISHLFQTYG RRTVEFVKGN GTKVIDNNGK QYLDFTSGIG VCNLGHCHPT VMKAVQEQLN DIWHISNLFT NSLQEEVASL LTENIALDYV FFCNSGAEAN EAALKLARKH TGKSLVVTCE QSFHGRTFGT MSATGQNKVK EGFGPLLPSF LHTPFNDIKA LKEVMNEEVA AVMVEVVQGE GGVIPADLSF LKEIETLCKK FGSLFIIDEV QTGIGRTGTL FAYEQMGIDP HIVTTAKALG NGIPVGAMIG RKELGTSFTA GSHGSTFGGN YVAMAAAKEV LQVSKRLSFL KEVQEKGEYV LQKLQEELQH VECIQNIRGK GLMVGIECTH EVASFIEQLE KEGLLVLQAG PNVIRLLPPL IVTNEELEQA VYMIKKVVCT KNVSII //