(data stored in SCRATCH zone)

SWISSPROT: C1ASZ9_RHOOB

ID   C1ASZ9_RHOOB            Unreviewed;       399 AA.
AC   C1ASZ9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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:BAH48931.1};
GN   OrderedLocusNames=ROP_06840 {ECO:0000313|EMBL:BAH48931.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48931.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48931.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48931.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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       {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; AP011115; BAH48931.1; -; Genomic_DNA.
DR   RefSeq; WP_012687933.1; NC_012522.1.
DR   ProteinModelPortal; C1ASZ9; -.
DR   STRING; 632772.ROP_06840; -.
DR   EnsemblBacteria; BAH48931; BAH48931; ROP_06840.
DR   KEGG; rop:ROP_06840; -.
DR   PATRIC; fig|632772.20.peg.745; -.
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; UP000002212; 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; -; 2.
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; 3.
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; C1ASZ9.
DR   SWISS-2DPAGE; C1ASZ9.
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:BAH48931.1};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_01107,
KW   ECO:0000256|SAAS:SAAS00768841, ECO:0000313|EMBL:BAH48931.1}.
FT   REGION      107    108       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   REGION      218    221       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     133    133       Pyridoxal phosphate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     136    136       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     275    275       N2-acetyl-L-ornithine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
FT   BINDING     276    276       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01107}.
FT   MOD_RES     247    247       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01107}.
SQ   SEQUENCE   399 AA;  40802 MW;  CD0EE0E457DDD622 CRC64;
     MTGTPELQQR WSGALMNTYG VPRVALTRGQ GAVLTDADGK EYVDFLAGIA VNILGHAHPA
     LIEAVTAQLS TLGHVSNLYA SEPAIELAEK LLSHLGAPGR VFFCNSGTEA NEAAFKLARA
     TGRSKIIAAE NSFHGRTMGA LALTGQAAKR APFEPMPPGV VHVPYGDLDA LDRAVDADTA
     AVFLEPMMGE GGVVVPPEGY LAGARQITAD RGALLVLDEV QTGIGRTGWF YAHQAVGIVP
     DVMTLAKGLG GGMPIGACVA TGAAADLFGP GKHGTTFGGN PVCASAALAV LRTIAEDDLI
     SRADTLGKAL SAGIEGLGHP LIDHVRGAGL LLGIVLTQDV APAVENSARE AGYLINAAQP
     GVVRLAPPLV LTDEQAEGFV AALPAILDNA QSAAQPGKQ
//

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