ID D3K124_BRABE Unreviewed; 500 AA.
AC D3K124;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
OS Branchiostoma belcheri (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7741 {ECO:0000313|EMBL:ADB91976.1};
RN [1] {ECO:0000313|EMBL:ADB91976.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20816894; DOI=10.1016/j.dci.2010.08.014;
RA Jing X., Zhang S.;
RT "An ancient molecule with novel function: Alanine aminotransferase as a
RT lipopolysaccharide binding protein with bacteriocidal activity.";
RL Dev. Comp. Immunol. 35:94-104(2011).
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 EMBL; GU354211; ADB91976.1; -; mRNA.
DR AlphaFoldDB; D3K124; -.
DR UniPathway; UPA00528; UER00586.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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:SF29; ALANINE TRANSAMINASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase {ECO:0000313|EMBL:ADB91976.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADB91976.1}.
FT DOMAIN 89..486
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 54877 MW; E524E41FDC72027E CRC64;
MASHLGNGPQ NGGPLGPAGQ TRAKVLTIDS MNPLVKKVEY AVRGPIVARA TELEKELERG
VPKPFKQVIK ANIGDAHAMG QKPITFLRQV ISLCVNPDLL DNESFPADAR ERARRILQGC
KGGSLGSYSD SVGVEVIRKG IAAYIERRDG FPSDPDNIFL STGASDAIKN MVKLLVRGEG
RDQTGVMIPI PQYPLYSAVV AELDAVQVNY YLNEDNNWAL NIAELERSVK EARDHCTPRV
LCVINPGNPT GQVLSKENVQ EIIKFAAREH LFLMADEVYQ DNIYAEGCAF HSFKKTLMEL
GPEYAGLELA SFHSTSKGYM GECGFRGGYM EVINMDPAVK LQLKKLVSTK LCPPVSGQAT
MDCVVNPPQP GEPSYESFIK EKTAVLTSLA ERAKLVAETF NSIEGVTCNT VQGAMYPFPR
IHLPRRAVEK AKSLGQSPDG FYALQLLEQA GICVVPGSGF GQREGTYHFR TTILPQPDKL
KIFMDAFTAF HNKFLQEYAD
//
