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Database: UniProt
Entry: A0A1I3QTC7_9GAMM
LinkDB: A0A1I3QTC7_9GAMM
Original site: A0A1I3QTC7_9GAMM 
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
//
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