ID A0A1J5HHB6_9CYAN Unreviewed; 457 AA.
AC A0A1J5HHB6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:OIP78456.1};
GN ORFNames=AUK48_01645 {ECO:0000313|EMBL:OIP78456.1};
OS Oscillatoriales cyanobacterium CG2_30_44_21.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales.
OX NCBI_TaxID=1805292 {ECO:0000313|EMBL:OIP78456.1, ECO:0000313|Proteomes:UP000185977};
RN [1] {ECO:0000313|EMBL:OIP78456.1, ECO:0000313|Proteomes:UP000185977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_44_21 {ECO:0000313|EMBL:OIP78456.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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:OIP78456.1}.
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DR EMBL; MNZA01000033; OIP78456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5HHB6; -.
DR STRING; 1805292.AUK48_01645; -.
DR Proteomes; UP000185977; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 457 AA; 51198 MW; 5DE01599096AA3AF CRC64;
MPDFSNDLPP NFSLDSHFLN LDRSNLEEMR RLGYQFVDLI MDSVLDTQKQ PFVKDESPFR
INIPEQGNDI SELIAEVRSQ ILPRTINFHN PNYVGHMDSI PAAITIWADA LISAINNNML
SYELAPIFTQ IESQLMQWFG ELFGLGSNCF GTLTAGGSLA NISGLLLARN WKQPQSRTRG
ASNHLVAFVS DAAHTSFEKA MNVIGLGKEN LIRVSTNDRG EVILEELEAA IQKAISLGKQ
PFFVAAIAGT TVTGAVDPIQ AVGAIAKRYD CWFHIDAAYG GAGIFTPKLQ PLFQGSDLAD
SITFNPQKWL WVSRTCAMII VKNKQHLIDG FDSELPYMNE STLNFGNLNL QGTRRTDSLK
LWLALKAMGT SGCRYLVERS LDRSEHLRQW IETSPDLELV CEPTLNIICL KSQNPQRTST
EIRQQWIDQG KLWLSLPLWK GDRILKAVVL HPYAFQD
//
