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Database: UniProt
Entry: A0A077JF99_9CYAN
LinkDB: A0A077JF99_9CYAN
Original site: A0A077JF99_9CYAN 
ID   A0A077JF99_9CYAN        Unreviewed;       388 AA.
AC   A0A077JF99;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   Name=aspC {ECO:0000313|EMBL:BAP17586.1};
GN   ORFNames=ETSB_0767 {ECO:0000313|EMBL:BAP17586.1};
OS   cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake Yunoko.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP17586.1, ECO:0000313|Proteomes:UP000031625};
RN   [1] {ECO:0000313|EMBL:BAP17586.1, ECO:0000313|Proteomes:UP000031625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP17586.1};
RX   PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA   Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA   Archibald J.M., Inagaki Y.;
RT   "Complete genome of a nonphotosynthetic cyanobacterium in a diatom reveals
RT   recent adaptations to an intracellular lifestyle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
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; AP012549; BAP17586.1; -; Genomic_DNA.
DR   RefSeq; WP_044106315.1; NZ_AP012549.1.
DR   AlphaFoldDB; A0A077JF99; -.
DR   STRING; 1228987.ETSB_0767; -.
DR   KEGG; ceo:ETSB_0767; -.
DR   HOGENOM; CLU_017584_4_3_3; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000031625; 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:BAP17586.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          32..381
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   388 AA;  42198 MW;  AC9869EE3074BA83 CRC64;
     MIKLATRVGK VSQSITLAIA AKAKAMKAQG IDVCSFSTGE PDFDTPQHIK EAAKLALNQG
     KTKYGPAAGE PTLRAAIAKK LRIDNNLNYT PDNIIVTNGG KQSLFNLMLA LIDPEDEVII
     PAPYWLSYPE MVKLATGTPV IVQTTTETSY KITPAQLRRA ITPKTKLFVL NSPSNPTGTV
     YSATEIKALA EVIIENNLWV VSDEIYEKIL YDGAEHLSIG AVSSEIFNRT IISNGFAKSY
     SMTGWRVGYL AAPIELIEAT NTIQSHSTSN VCTFAQYGAI AALEESQDSV EQMLQAFTKR
     RQVILDGIMT IPHLSCPTPM GAFYVFADIS HTKISSLDFC EALLESQKVT AVPGKVFGTD
     NCIRLSYATD LTSIEKGIDR LAQFVSSL
//
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