(data stored in SCRATCH zone)

SWISSPROT: C3MFB6_SINFN

ID   C3MFB6_SINFN            Unreviewed;       431 AA.
AC   C3MFB6;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
DE   RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107};
DE            Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107};
DE            EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107};
GN   Name=argD {ECO:0000256|HAMAP-Rule:MF_01107,
GN   ECO:0000313|EMBL:ACP23953.1};
GN   OrderedLocusNames=NGR_c01510 {ECO:0000313|EMBL:ACP23953.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23953.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23953.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-
CC       acetyl-L-glutamate 5-semialdehyde + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 4/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- MISCELLANEOUS: May also have succinyldiaminopimelate
CC       aminotransferase activity, thus carrying out the corresponding
CC       step in lysine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. ArgD subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01107}.
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DR   EMBL; CP001389; ACP23953.1; -; Genomic_DNA.
DR   RefSeq; WP_012706738.1; NC_012587.1.
DR   RefSeq; YP_002824706.1; NC_012587.1.
DR   ProteinModelPortal; C3MFB6; -.
DR   STRING; 394.NGR_c01510; -.
DR   EnsemblBacteria; ACP23953; ACP23953; NGR_c01510.
DR   GeneID; 7790730; -.
DR   KEGG; rhi:NGR_c01510; -.
DR   PATRIC; fig|394.7.peg.2946; -.
DR   eggNOG; ENOG4105C8Y; Bacteria.
DR   eggNOG; COG4992; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00821; -.
DR   OMA; GIATCTL; -.
DR   OrthoDB; POG091H03ZS; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000001054; 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-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00707; argD; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MFB6.
DR   SWISS-2DPAGE; C3MFB6.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768889, ECO:0000313|EMBL:ACP23953.1};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS00768842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768841, ECO:0000313|EMBL:ACP23953.1}.
FT   REGION      130    131       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   REGION      248    251       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     163    163       Pyridoxal phosphate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     166    166       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     305    305       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     306    306       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01107}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
SQ   SEQUENCE   431 AA;  45775 MW;  AFD8FA8747FCECF6 CRC64;
     MGIVPAPPQG GIFDFYRAES PVAMPTTKET LTMAATTPLY DTYLRAPLRF ERGEGVWLIA
     EDGTRYLDFA AGVAVNSLGH AHPHLVEALK AQAEKLWHVS NLYDVPGQES LARRLTAVTF
     ADRVFFTNSG AEALECAIKT ARRYHFAKGH PERFHVITFE GAFHGRTIAT IAAGGQQKYI
     EGFGPKAPGF YQVPFGDIAA VKNAINDETA AILIEPIQGE GGIRLASKEF MQELRALCDE
     YGLLLILDEV QCGVGRTGKL FAHEWSGITP DIMAVAKGIG GGFPLGACLA TEAAAAGMVA
     GTHGSTYGGN PLAMAVGNAV LDVVLAEGFL ENVRDVALVF RQGLASLKDR FPDVIEEIRG
     DGLMLGIKAK VPCADVLKAI RAEKLLAVPA GENVLRLLPP LITTAAEARE GLARLERAAE
     AVRAASGTAA A
//

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