ID M7P7G5_PNEMU Unreviewed; 405 AA.
AC M7P7G5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=PNEG_01968 {ECO:0000313|EMBL:EMR09785.1};
OS Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS (Pneumocystis carinii f. sp. muris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR09785.1, ECO:0000313|Proteomes:UP000011958};
RN [1] {ECO:0000313|Proteomes:UP000011958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMR09785.1}.
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DR EMBL; AFWA02000009; EMR09785.1; -; Genomic_DNA.
DR RefSeq; XP_007873946.1; XM_007875755.1.
DR AlphaFoldDB; M7P7G5; -.
DR STRING; 1069680.M7P7G5; -.
DR GeneID; 19895662; -.
DR VEuPathDB; FungiDB:PNEG_01968; -.
DR eggNOG; KOG1412; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR OMA; MGFEMFC; -.
DR OrthoDB; 1123851at2759; -.
DR Proteomes; UP000011958; Unassembled WGS sequence.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF55; GLUTAMATE OXALOACETATE TRANSAMINASE 1, ISOFORM B; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000011958}.
FT DOMAIN 31..398
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 405 AA; 46246 MW; 256BE335F5E37FBA CRC64;
MENSLFEDVP YIEKDVIFEL MRLYKDDKFE KKVDLGIGVY RDNYGKPCLL SSVRKAESII
ITDPNYNHEY LPIDGLPSFI EASKKLVFGE NSPLINSGCV SSVQTISGTG ANHLGSLFIS
LFNKGAVCYF SRPTWSNHDP IWKHAGLTIR EYPYFDESTC GFDFEGMITT LQEAPENSII
LLHVCGHNPT GVDPTREQWI KICDVMKEKK LFPFFDFAYQ GFVSGDIDED AWPIRHFSER
GFELCVCHSF SKSFGLYGER CGCFHLVVKS PDIAKNVHSQ LVRIQRNEIS SPPSYGAKIV
SLILNNEQLT QEWKKNILEI SNRIKEIRKL FYQELIRLGT PGSWEHIINQ VGMFSYLSLS
EKDICRLVNE FHIYIPSNGR ISISGLRTGN LEYVARAFDT VVRDL
//
