ID S9Y3E7_CAMFR Unreviewed; 401 AA.
AC S9Y3E7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Tyrosine aminotransferase {ECO:0000256|PIRNR:PIRNR000517};
DE Short=TAT {ECO:0000256|PIRNR:PIRNR000517};
DE EC=2.6.1.5 {ECO:0000256|PIRNR:PIRNR000517};
GN ORFNames=CB1_000691012 {ECO:0000313|EMBL:EPY81976.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY81976.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY81976.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
CC -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC tyrosine to p-hydroxyphenylpyruvate. {ECO:0000256|PIRNR:PIRNR000517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC Evidence={ECO:0000256|PIRNR:PIRNR000517};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR000517, ECO:0000256|PIRSR:PIRSR000517-1};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC {ECO:0000256|PIRNR:PIRNR000517}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR000517}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|PIRNR:PIRNR000517}.
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DR EMBL; KB016958; EPY81976.1; -; Genomic_DNA.
DR AlphaFoldDB; S9Y3E7; -.
DR UniPathway; UPA00139; UER00338.
DR Proteomes; UP000030684; Unassembled WGS sequence.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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 InterPro; IPR011715; Tyr_aminoTrfase_ubiquitination.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR NCBIfam; TIGR01265; tyr_nico_aTase; 1.
DR PANTHER; PTHR45744; TYROSINE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR45744:SF2; TYROSINE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF07706; TAT_ubiq; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EPY81976.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR000517};
KW Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW Transferase {ECO:0000313|EMBL:EPY81976.1}.
FT DOMAIN 134..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 227
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000517-1"
SQ SEQUENCE 401 AA; 44628 MW; B442779512CF350D CRC64;
MDPYVIQMHS KGNLPSVLDV HVNVAGKSSM LGKMKGKKAR WSVRPSEMSN KTFNPIRAIV
DSMKVQPNPN KTTIALSIGD PTVFGNLPTD PEVTQAMKDA LDSGKYNGYA PSVGYLSSRE
EVASYYHCPK APLEAKPEKS WEIDLKQLES LIDEKTACLV VNNPSNPCGS VFSRSHLRKI
LAVAARQCVP ILADEIYGDM VFSNSKFEPL ATLSSNVPIL SCGGLAKRWL VPGWRLGWIL
IHDRRDIFGN EIRDGLVKLS QRILGPCTLV QGALKSILHR TPQEFYHNTL SFLKSNADLC
YGALAAIPGL RPIRPSGAMY LMVGIEMEHF PEFENDVAFT ERLVAEQSVQ CLPATCFEYP
NFFRVVITVP EVMMLEACSR IQEFCEQHYH CAEGSQEECD K
//
