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
//