ID   B0X4U1_CULQU            Unreviewed;       549 AA.
AC   B0X4U1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=6047630 {ECO:0000313|EnsemblMetazoa:CPIJ014256-PA};
GN   ORFNames=CpipJ_CPIJ014256 {ECO:0000313|EMBL:EDS40556.1},
GN   CpipJ_CPIJ017506 {ECO:0000313|EMBL:EDS45787.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS40556.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS40556.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ014256-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ014256-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   EMBL; DS232354; EDS40556.1; -; Genomic_DNA.
DR   EMBL; DS232797; EDS45787.1; -; Genomic_DNA.
DR   RefSeq; XP_001864663.1; XM_001864628.1.
DR   RefSeq; XP_001867887.1; XM_001867852.1.
DR   AlphaFoldDB; B0X4U1; -.
DR   STRING; 7176.B0X4U1; -.
DR   EnsemblMetazoa; CPIJ014256-RA; CPIJ014256-PA; CPIJ014256.
DR   EnsemblMetazoa; CPIJ017506-RA; CPIJ017506-PA; CPIJ017506.
DR   GeneID; 6051448; -.
DR   KEGG; cqu:CpipJ_CPIJ014256; -.
DR   KEGG; cqu:CpipJ_CPIJ017506; -.
DR   VEuPathDB; VectorBase:CPIJ014256; -.
DR   VEuPathDB; VectorBase:CPIJ017506; -.
DR   VEuPathDB; VectorBase:CQUJHB003437; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_1_1; -.
DR   InParanoid; B0X4U1; -.
DR   OMA; FGFECPP; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
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   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   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EDS40556.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDS40556.1}.
FT   DOMAIN          138..534
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   549 AA;  59898 MW;  2F9C35A8F29F4747 CRC64;
     MSLSQVLNVC PKGASLVAAT GRRNVGRIST LLLSSSVGQQ CNASATSSSV LLSADPLVFS
     ANGTSNSRSM STRCVTVDNI NPAIKLMEYA VRGPLVIRAG VIEKELEQGA KKPFTEVIRA
     NIGDCHAMGQ QPITFLRQVL GLVSYPPLFD DKSIPEDAKQ RARDILKGCK GGSVGSYTDS
     NGIEVIRQHV AQYIQDRDGG IPSDPANIIL SAGASGGIKV LMSLLRCPID GKKPGVMIPI
     PQYPLYSATI AEFEMEQCGY YLDEANKWGL DITELKRSLA EAKTKCAPRI LVVINPGNPT
     GQVLSKENIQ EIIKFAHQEK LVLFADEVYQ DNVYEKGSQF HSFKKVLMEM GAPYNTMELC
     SFMSCSKGYM GECGIRGGYA EIVNLCPDVK AMLLKCISAQ LCPTTIGQAC MDVVVHPPRK
     GEPSYELFMK EKTAVLESLK VRAEMVAETF NSIEGFSCNP VQGAMYAFPQ IRLPAKAIEA
     AKKAGQAPDV FYAFQLLEQT GICIVPGSGF GQRPGTYHFR TTILPQPAKL KEMLGKFRSF
     HEKFLQEYK
//