(data stored in ACNUC14238 zone)

HOGENOM: SCHPO_1_PE1003

ID   SCHPO_1_PE1003                       STANDARD;      PRT;   421 AA.
AC   SCHPO_1_PE1003; O14209;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Uncharacterized aminotransferase C6B12.04c; EC=2.6.1 -;
DE   (SCHPO_1.PE1003).
GN   ORFNames=SPAC6B12.04c;
OS   SCHIZOSACCHAROMYCES POMBE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SCHPO_1.PE1003.
CC       Schizosaccharomyces pombe chromosome I EF1 full sequence 1..5579133
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:YDT4_SCHPO
CC   -!- COFACTOR: Pyridoxal phosphate (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -!- GENE_FAMILY: HOG000223045 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Schizosaccharomyces_pombe;SPAC6B12.04C;SPAC6B12.04C-1;SPAC6B12.04C-1.
DR   UniProtKB/Swiss-Prot; O14209; -.
DR   EMBL; CU329670; CAB11066.1; -; Genomic_DNA.
DR   PIR; T39011; T39011.
DR   RefSeq; NP_593759.1; NM_001019189.1.
DR   ProteinModelPortal; O14209; -.
DR   STRING; O14209; -.
DR   EnsemblFungi; SPAC6B12.04c-1; SPAC6B12.04c-1; SPAC6B12.04c.
DR   GeneID; 2543228; -.
DR   KEGG; spo:SPAC6B12.04c; -.
DR   NMPDR; fig|4896.1.peg.3729; -.
DR   GeneDB_Spombe; SPAC6B12.04c; -.
DR   eggNOG; fuNOG04782; -.
DR   GeneTree; EFGT00050000001332; -.
DR   OMA; PRLANIV; -.
DR   OrthoDB; EOG4WHCV4; -.
DR   PhylomeDB; O14209; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-001416-MON; -.
DR   ArrayExpress; O14209; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_Spombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_Spombe.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001176; ACC_synthase.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   HOGENOMDNA; SCHPO_1.PE1003; -.
KW   SPAC6B12.04ccc7236820036002503210000011;
KW   O14209;
KW   Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   421 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAFRGIRPSN KVAASRPDVW TLVNQATAEC KVPPVSLSQG FFNYNPPKFV LDAAKKSIDE
     VACNQYSHTR GRPSLRKALS EAYSPYFKRT LNPDTEIVVT AGANEGFFSV FAAFLNPGDE
     VIVMEPFFDQ YISNITMNGG VPVYVPIIPP EEGSVKPVSA GAWKLDMNKL RNAITEKTKM
     IVINTPHNPL GKIFSEEELN EIADLVLKHN LLVVSDEVYD RLSFVPFVRL ATLRPELFKH
     VVTVGSGGKT FGCTGWRVGW LIGDESLIKY SAAAHTRICF AVNSPCQEAL AIAFGEAEKH
     NYYEEYKSSY KKRFEILAKA FDQLEIPYTI PDGSYYTMAN FSKLKLPKDY PFPEEIANRP
     RDFKLCYWIL KEIGVATIPP TEFYTDEDAP VAENYLRFAF CKTFETLEEA ARRLQKLKDY
     F
//

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