(data stored in ACNUC8465 zone)

SWISSPROT: C5DC59_LACTC

ID   C5DC59_LACTC            Unreviewed;       463 AA.
AC   C5DC59;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 54.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000256|RuleBase:RU365036};
DE            EC=2.6.1.13 {ECO:0000256|RuleBase:RU365036};
GN   OrderedLocusNames=KLTH0B00220g {ECO:0000313|EMBL:CAR21369.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21369.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21369.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-
CC         glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, 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-glutamate
CC       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; CU928166; CAR21369.1; -; Genomic_DNA.
DR   RefSeq; XP_002551808.1; XM_002551762.1.
DR   STRING; 381046.XP_002551808.1; -.
DR   EnsemblFungi; CAR21369; CAR21369; KLTH0B00220g.
DR   GeneID; 8290626; -.
DR   KEGG; lth:KLTH0B00220g; -.
DR   HOGENOM; HOG000020206; -.
DR   InParanoid; C5DC59; -.
DR   KO; K00819; -.
DR   OMA; GGARQYC; -.
DR   OrthoDB; 145181at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000002036; Chromosome B.
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:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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; C5DC59.
DR   SWISS-2DPAGE; C5DC59.
KW   Aminotransferase {ECO:0000256|RuleBase:RU365036};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transferase {ECO:0000256|RuleBase:RU365036}.
FT   COILED          357..377
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   463 AA;  50500 MW;  4FF0C239BCA10370 CRC64;
     MILARGKVAG LRRVFHHGGA FLASSQAFKM STLNTDLSSE TTVQYEKAYS AHNYHPLPVV
     FQKAKGAKVW DPEGKQYLDF LSAYSAVNQG HCHPDIIAAL VDQASKLTLS SRAFSNNVFS
     AFAKFITEYF RYESVLPMNT GAEAVETGLK LARRWGYMKK GIPENEAIIL GAKDNFHGRT
     LGALSLSTDE EARKFFGPFL ESITAKIPGT DGQYLRYGNI EDVELAFKNA GDRIAAILLE
     PIQGEAGIVV PPVEYLQKVQ ELCRKYNVLL ICDEIQTGIA RTGKMLCYEH SPNVKPDVIL
     LGKAISGGIL PVSCVLSSKE IMGCFEPGSH GSTYGGNPLS SRVAIAALEV VKKENLVERA
     KTLGEFFQSE LKKLQQEAGG IISDVRGRGL LTAIVIDPSK SNGRTAWDLC LLMKDQGVLA
     KPTHDHIIRL APPLVISKED LMKGVEAIRA SLKLLPNAAK SNH
//

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