(data stored in SCRATCH zone)

SWISSPROT: Q6BMF0_DEBHA

ID   Q6BMF0_DEBHA            Unreviewed;       435 AA.
AC   Q6BMF0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000256|RuleBase:RU365036};
DE            EC=2.6.1.13 {ECO:0000256|RuleBase:RU365036};
GN   OrderedLocusNames=DEHA2F06006g {ECO:0000313|EMBL:CAG88948.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88948.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88948.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid
CC         + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877,
CC         ChEBI:CHEBI:35179, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066,
CC         ChEBI:CHEBI:59869; EC=2.6.1.13;
CC         Evidence={ECO:0000256|RuleBase:RU365036};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU365036};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000256|RuleBase:RU365036}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CR382138; CAG88948.2; -; Genomic_DNA.
DR   RefSeq; XP_460621.2; XM_460621.1.
DR   STRING; 4959.XP_460621.2; -.
DR   EnsemblFungi; CAG88948; CAG88948; DEHA2F06006g.
DR   GeneID; 2903125; -.
DR   KEGG; dha:DEHA2F06006g; -.
DR   HOGENOM; HOG000020206; -.
DR   InParanoid; Q6BMF0; -.
DR   KO; K00819; -.
DR   OMA; HSAWDLC; -.
DR   OrthoDB; 145181at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IEA:EnsemblFungi.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006591; P:ornithine metabolic process; IEA:EnsemblFungi.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR010164; Orn_aminotrans.
DR   InterPro; IPR034758; Orn_aminotrans_mito.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11986:SF18; PTHR11986:SF18; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01885; Orn_aminotrans; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMF0.
DR   SWISS-2DPAGE; Q6BMF0.
KW   Aminotransferase {ECO:0000256|RuleBase:RU365036};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transferase {ECO:0000256|RuleBase:RU365036}.
SQ   SEQUENCE   435 AA;  46992 MW;  C4C941349AD5A69C CRC64;
     MTSPNFNISS ELAVKYETDY SAHNYHPLPV VFTKAKGAHV WDPEGKEYLD FLSAYSAVNQ
     GHCHPKIVEA LVDQASKLTL CSRAFSSDVF GVFAKYITEY FDYEMVLPMN TGAEAVETGL
     KLARRWGYVE KGIPEDEAVI LSAVNNFHGR TLGVISMSTD PEATSKFGPY LQGVGPQIPG
     EPKGTLLRYG EIEDVEKAFN NAGDKIAAIL LEPIQGEAGI VVPPEGYLTK VQALCKKHNV
     LLICDEIQTG VARTGKMLCY EHSANVKPDV ILLGKAISGG VMPVSAVLSS KKIMLCLEPG
     SHGSTYGGNP LACRVATAAL QVVKDENLVD RSNKLGELLR SKLEELKAKS NGVISEVRGK
     GLLCAIVIDD SKTNGRTAWD LCLLMKDHGV LAKPTHDHII RLAPPLVISE ADLLKGVDSI
     EKSLSELNDA PKAAH
//

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