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Database: UniProt/TrEMBL
Entry: A9RXP9_PHYPA
LinkDB: A9RXP9_PHYPA
Original site: A9RXP9_PHYPA 
ID   A9RXP9_PHYPA            Unreviewed;       533 AA.
AC   A9RXP9;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   20-JUN-2018, entry version 64.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=PHYPADRAFT_105373 {ECO:0000313|EMBL:EDQ76428.1};
OS   Physcomitrella patens subsp. patens (Moss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae;
OC   Physcomitrella.
OX   NCBI_TaxID=3218;
RN   [1] {ECO:0000313|EMBL:EDQ76428.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B.,
RA   Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K.,
RA   Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A.,
RA   Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R.,
RA   Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J.,
RA   Sanderfoot A., Schween G., Shiu S.H., Stueber K., Theodoulou F.L.,
RA   Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L.,
RA   Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R.,
RA   Grigoriev I.V., Quatrano R.S., Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the
RT   conquest of land by plants.";
RL   Science 319:64-69(2008).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; DS544923; EDQ76428.1; -; Genomic_DNA.
DR   RefSeq; XP_001758922.1; XM_001758870.1.
DR   UniGene; Ppa.7594; -.
DR   ProteinModelPortal; A9RXP9; -.
DR   STRING; 3218.PP1S34_308V6.2; -.
DR   EnsemblPlants; PP1S34_308V6.2; PP1S34_308V6.2; PP1S34_308V6.
DR   Gramene; PP1S34_308V6.2; PP1S34_308V6.2; PP1S34_308V6.
DR   KEGG; ppp:PHYPADRAFT_105373; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   InParanoid; A9RXP9; -.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     281    281       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   533 AA;  59605 MW;  C6ACFAFED00EDFBD CRC64;
     MVLSICKSMK ETKGHDTIDS MFASRYAQAE LPRFEIPTQE TPKDVAYQII SDELMLDGNP
     RLNLASFVTT WMEPECDKLI MAALNKNYID MDEYPITTEL QDRCVNMVAR LFNAPIGEGE
     QAVGAGTVGS SEAIMLAGLA FKRKWQLERK AAGKPWDKPN MVTGANVQVC WEKFARYFEV
     ELREVTLKED YYVMDPHRAV ELVDENTICV CAILGSTYNG EFEDVQLLND LLEKKNQELG
     LNVPIHVDAA SGGFVVPFIY PDIVWDFRLP LVKSINVSGH KYGLVYAGIG WVVWRNKEDL
     PEELIFHVNY LGADQPTFTL NFSKGASQVI AQYYQLIRLG FNGYKSIMTN CAMNAKILTQ
     AIENLGRFKI LSKEVGVPLV AFSLLDSSNY TEFDISDGLR RYGWTVPAYT MAPDAQHVTL
     LRVVVREDFS RSLANRLVTD IKRVLDHFDA RPPKLIEVVT AAVAQENREA NLDLPTTPDA
     VKATAAFNDI VVEGHHGGKK KQQHGHGHGH HGPIATTTAT AKTTTARNPP FTR
//
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