ID K9Z6I0_CYAAP Unreviewed; 389 AA.
AC K9Z6I0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Cyan10605_2267 {ECO:0000313|EMBL:AFZ54352.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ54352.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP003947; AFZ54352.1; -; Genomic_DNA.
DR RefSeq; WP_015220076.1; NC_019776.1.
DR AlphaFoldDB; K9Z6I0; -.
DR STRING; 755178.Cyan10605_2267; -.
DR KEGG; can:Cyan10605_2267; -.
DR PATRIC; fig|755178.3.peg.2408; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_3; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000010480; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:AFZ54352.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010480};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AFZ54352.1}.
FT DOMAIN 33..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 389 AA; 42513 MW; B5C8CBC105B6C861 CRC64;
MTQLADRISQ VTPSITLTIS AKAKAMKAEG LDVCSFSAGE PNFDTPNHIK EAAKKALDEG
KTRYGAAAGE LALRNAIASK LQRDNNLNYQ AENVIVTNGG KHALFNLIFA LIEPEDEVII
PVPYWLSYPE MVTLAGGKSI FVTTSAENNY KITPEQLESA ITPKTKLLIL NSPSNPTGAV
YTPEEIHSLA EIVIKHDILV VSDEIYEKIL YEGATHLSIG AVSEEVFKRT IVCNGFAKAY
SMTGWRVGYI AGSVDIIKGM TTIQSHTTSN VCTFAQYGAI AALESSQDCV KEMLEAFTER
RKFMYSAIQS IQGISCPLPY GAFYLFVDIS STGLKSLEFC EKLLQQEKVA AIPGIAFGDD
NCIRLSYATD MTTIEKGINR LNNFIQSIN
//
