ID A0A1I3QTC7_9GAMM Unreviewed; 593 AA.
AC A0A1I3QTC7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:SFJ36759.1};
GN ORFNames=SAMN05421680_1084 {ECO:0000313|EMBL:SFJ36759.1};
OS Xenorhabdus mauleonii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351675 {ECO:0000313|EMBL:SFJ36759.1, ECO:0000313|Proteomes:UP000198919};
RN [1] {ECO:0000313|Proteomes:UP000198919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17908 {ECO:0000313|Proteomes:UP000198919};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; FORG01000008; SFJ36759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3QTC7; -.
DR STRING; 351675.SAMN05421680_1084; -.
DR Proteomes; UP000198919; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR022517; Asp_decarboxylase_pyridox.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
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 389
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 593 AA; 66415 MW; AAAC5F16C5C9372B CRC64;
MDLELRQGGK GMHPRDVWIA RHKHMNDIIS DPKRQTMLYS LDSLNCGDVD KTTLHPSNQD
PQEWQALLEQ FFPHGSDEGL LELETSIASD PVTYCLHELN KPVKELTELE ANFSSVIIPE
LPVNGSTYAR HLREDILNQV VPVSSPAFVG HMTSALPQHL PAIGKILTAL NQNVVKLETS
HVLTALERQV LGMMHKLVYN CDETFYKQWL HNGDYALATF CSGGTLANLT AMWACRNQLL
PADGDFAGLA REGLARGLIH YGYSGLAILV SELGHYSLKK TVDVLGLGQD SLIKIETDSN
GRICTNALLA KLQELRQRNI KPMAIIGIAG TTETGSIDPL NTLADIAEQE QCHFHVDAAW
GGASLLSERH RHLFAGIERA DSVTIDAHKQ MYVPMGTGMV LFRQPNLVSA ISQHANYIVR
KGSKDLGRHT LEGSRCAMSL MLHSNFHLLG RRGFAQLIDA SIEKAQQFAD LIRQQEDFEL
ISEPELCLLT YRYMPPRVLQ TLRTAAESEK QKLHDELNAL NQHIQTMQWT AGQSFVSRTT
LHPTQWDRQP TTVLRVVLAN PLTTMEILED MLKEQRQLAQ QSPHWQTLQA LIH
//