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Database: UniProt
Entry: W1QCA2_OGAPD
LinkDB: W1QCA2_OGAPD
Original site: W1QCA2_OGAPD 
ID   W1QCA2_OGAPD            Unreviewed;       376 AA.
AC   W1QCA2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=alanine--glyoxylate transaminase {ECO:0000256|ARBA:ARBA00013049};
DE            EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049};
GN   ORFNames=HPODL_04289 {ECO:0000313|EMBL:ESW98676.1};
OS   Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS   Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW98676.1, ECO:0000313|Proteomes:UP000008673};
RN   [1] {ECO:0000313|EMBL:ESW98676.1, ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA   Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT   DL1.";
RL   BMC Genomics 14:837-837(2013).
RN   [2] {ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RA   Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA   Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT   "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC       ECO:0000256|RuleBase:RU004075}.
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:ESW98676.1}.
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DR   EMBL; AEOI02000008; ESW98676.1; -; Genomic_DNA.
DR   RefSeq; XP_013934559.1; XM_014079084.1.
DR   AlphaFoldDB; W1QCA2; -.
DR   STRING; 871575.W1QCA2; -.
DR   GeneID; 25773717; -.
DR   KEGG; opa:HPODL_04289; -.
DR   eggNOG; KOG2862; Eukaryota.
DR   HOGENOM; CLU_027686_5_2_1; -.
DR   OMA; VTITYNE; -.
DR   OrthoDB; 3183437at2759; -.
DR   Proteomes; UP000008673; Chromosome V.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   PANTHER; PTHR21152:SF24; SERINE--PYRUVATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ESW98676.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW   Transferase {ECO:0000313|EMBL:ESW98676.1}.
FT   DOMAIN          22..308
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   376 AA;  40634 MW;  1D89460662D029CC CRC64;
     MSRKLTFIPG PVEFSDAVLN AMSTPSQSHS SPEFTQVFQE ALKNTRKVFK STDPETQPFV
     LSGSGTLGWE LVGANLVSRS EAVLVVSTGF FSEHFAEALQ VYTDNVDIVG AEVFGDAVKL
     PAIEAKLKAK SYGVITVTQT DTSSGVLSNV KEIAALVKKV SPNTLIVVDA VCATACEELE
     FDAWGIDFVL TGSQKALGCP SGLSISYASK RALDKALAHK PVSYYASIPR WLPVMRAFEN
     GSPAYFATPA VQLVHAYNVA LKEVLSPSLE ERIKAHAEAS NKFKNNLESL GVKLVTVSRD
     VAAHGLTTAY YPDGVDGPTF LSKVRDNGFT LATGIYKDYK DKYFRVGHMG VSAVGERKQE
     LDQCFEAIAK ALRESK
//
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