ID   ALAT2_DANRE             Reviewed;         549 AA.
AC   Q6NYL5; A2BII0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Alanine aminotransferase 2-like;
DE            Short=ALT2;
DE            EC=2.6.1.2;
DE   AltName: Full=Glutamate pyruvate transaminase 2;
DE            Short=GPT 2;
DE   AltName: Full=Glutamic--alanine transaminase 2;
DE   AltName: Full=Glutamic--pyruvic transaminase 2;
GN   Name=gpt2l; Synonyms=gpt2; ORFNames=im:6791811, si:ch211-261f3.4;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transamination between alanine and
CC       2-oxoglutarate to form pyruvate and glutamate. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NYL5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NYL5-2; Sequence=VSP_029840;
CC   -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM14165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX928742; CAM14165.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC061955; AAH61955.1; -; mRNA.
DR   EMBL; BC066543; AAH66543.1; -; mRNA.
DR   RefSeq; XP_017213488.1; XM_017357999.1. [Q6NYL5-1]
DR   AlphaFoldDB; Q6NYL5; -.
DR   SMR; Q6NYL5; -.
DR   STRING; 7955.ENSDARP00000121415; -.
DR   PaxDb; 7955-ENSDARP00000121415; -.
DR   GeneID; 403086; -.
DR   AGR; ZFIN:ZDB-GENE-050302-11; -.
DR   CTD; 2875; -.
DR   ZFIN; ZDB-GENE-050302-11; gpt.
DR   eggNOG; KOG0258; Eukaryota.
DR   InParanoid; Q6NYL5; -.
DR   OrthoDB; 5472891at2759; -.
DR   PhylomeDB; Q6NYL5; -.
DR   Reactome; R-DRE-8964540; Alanine metabolism.
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:Q6NYL5; -.
DR   Proteomes; UP000000437; Chromosome 2.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042851; P:L-alanine metabolic process; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Alternative splicing; Aminotransferase; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..549
FT                   /note="Alanine aminotransferase 2-like"
FT                   /id="PRO_0000247534"
FT   MOD_RES         367
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..44
FT                   /note="MLSKRSLRVLKWGRCEAAYAAAYPKVPDWVLNFSPLPSLSSPHR -> ADLS
FT                   LLSVVSATEEAPLLHFW (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_029840"
FT   CONFLICT        57
FT                   /note="M -> L (in Ref. 2; AAH66543/AAH61955)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   549 AA;  61092 MW;  633DDE9C6F3305D9 CRC64;
     MLSKRSLRVL KWGRCEAAYA AAYPKVPDWV LNFSPLPSLS SPHRDFSAFP AAQSEHMQQK
     MSENGAIPRQ GKVLTVDTMN ANVKKVDYAV RGPIVQRAVQ IEKELKEGVK KPFDEVIKAN
     IGDAHAMGQR PITFFRQVMA LCTYPQLLDD NKFPEDAKNR ARRILQSCGG NSIGAYTTSQ
     GIDCVRQDVA KYIERRDGGI PSDPDNIYLT TGASDGIVTI LKLLTAGEGL TRTGVMISIP
     QYPLYSASIA ELGAVQINYY LNEEKCWSLD ISELQRSLQA ARKHCNPRVL CIINPGNPTG
     QVQSRQCIED VIQFAAKENL FLMADEVYQD NVYAKGCEFH SFKKVLFEMG PEYSKKVELA
     SFHSTSKCYM GECGFRGGYM EVINMDADVK AQLTKLVSVR LCPPAPGQAL MDLVVNPPQP
     GEPSHQTFMQ ERTAVLSALA EKAKLTEQIL NTVPGISCNP VQGAMYSFPR ITLPERAISE
     AKAKGQAPDM FYCMKLLEET GICLVPGSGF GQREGTYHFR MTILPPTDKL KLMLNKLKDF
     HQRFTQQYS
//