ID   G5BIW6_HETGA            Unreviewed;       489 AA.
AC   G5BIW6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Glutamate decarboxylase-like protein 1 {ECO:0000313|EMBL:EHB09227.1};
GN   ORFNames=GW7_21442 {ECO:0000313|EMBL:EHB09227.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB09227.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB09227.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; JH170539; EHB09227.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5BIW6; -.
DR   STRING; 10181.G5BIW6; -.
DR   InParanoid; G5BIW6; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 3.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45677:SF1; ACIDIC AMINO ACID DECARBOXYLASE GADL1; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813}.
SQ   SEQUENCE   489 AA;  55955 MW;  A6FE097B1E713D8F CRC64;
     MALPSKKNAI LVDGVVLNGP TTDIRAGEKF VEEACRLIME EVVLKATDVN EKVCEWQSPE
     QLKQLLDLEM RDTGEPHDRL LQLCRDVIRF SVKTNHPRFF NQLYAGLDYY SLVGRFMTEA
     LNPSVYTYEV SPVFLLVEEA VVKKMIEFIG WQEGDGIFNP GGSVSNMYAM NLARYKYCPD
     IKEKGLSGLP RLILFTSAEC HYSMKKSASF LGIGTENVCF VETDGRGKMI PEELEKQVLQ
     ARKEGAAPFL VCATSGTTVL GSFDPLEEIA DVCDRHGLWL HVDDLLKKCY SAEASYLFQQ
     DKFYDVSYDT GDKSIQCSRR PDAFKFWMTW KALGTLGLEE RVNRALALSR YLVDEIKKRD
     GFKLLMEPEY ANICFWYIPP SLREMEEGPE FWEKVNLEGR VHIYISICNV AMKFNTCHVV
     YLVDRKDAVK LLVAPAIKER MMKKGSLMLG YQPHRGKVNF FRQVVINPQV SREDMDFLLD
     EIDLLGRDM
//