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Database: UniProt
Entry: H2TVB7_TAKRU
LinkDB: H2TVB7_TAKRU
Original site: H2TVB7_TAKRU 
ID   H2TVB7_TAKRU            Unreviewed;       548 AA.
AC   H2TVB7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000028626.2, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000028626.2, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000028626.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00024611};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00025708}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000256|ARBA:ARBA00025785}.
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DR   AlphaFoldDB; H2TVB7; -.
DR   STRING; 31033.ENSTRUP00000028626; -.
DR   Ensembl; ENSTRUT00000028742.3; ENSTRUP00000028626.2; ENSTRUG00000011343.3.
DR   eggNOG; KOG0258; Eukaryota.
DR   GeneTree; ENSGT00940000155265; -.
DR   InParanoid; H2TVB7; -.
DR   OMA; IGDPNLF; -.
DR   TreeFam; TF300839; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000005226; Chromosome 22.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 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; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF468; ALANINE AMINOTRANSFERASE 2-LIKE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          154..535
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          24..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  60588 MW;  7549269A49592E02 CRC64;
     MQLLSPRNLS FLGRGRTELF AVSGAPKRAG DGPRGRALNS SPVSSRTISS VSETRRGLPR
     EKMTENGVSS RAKVLTIDTM NPTVKKVEYA VRGPIVQRAV ELERELSQGV KKPFAEVIKA
     NIGDAHAMGQ QPITFFRQVL ALCSYPELLN DSTFPEDAKS RARRILQSCG GNSLGSYSAS
     QGIESVRQDV ARYIERRDGG VPCAPDNIYL TTGASDGIVT MLKLLVCGEG ATRTGVMISI
     PQYPLYSAAL AELGAVQVNY YLNEEKCWSL DISELQRSVD EARTHCNPRA LCIINPGNPT
     GQVQSRQCIE DVIRFAAKER LFLMADEVYQ DNVYADGCQF HSFKKVLFEM GPEYSSTVEL
     ASFHSTSKCY MGECGFRGGY MEIINMDNEV KAQLTKLVSV RLCPPVPGQA LMDLVVNPPQ
     PGEPSYDNFI KERTATLSVL AEKAKLTEQV LNTVEGIRCN PVQGAMYSFP RISIPEKAVK
     EANGQQPDMF YCMRLLEETG ICLVPGSGFG QKDGTYHFRM TILPPTDKLK ILLDKVKEFH
     HKFTQKYS
//
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