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Database: UniProt
Entry: W7KLB3_9CREN
LinkDB: W7KLB3_9CREN
Original site: W7KLB3_9CREN 
ID   W7KLB3_9CREN            Unreviewed;       453 AA.
AC   W7KLB3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE            EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
GN   Name=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712};
GN   ORFNames=ASUL_05743 {ECO:0000313|EMBL:EWG06998.1}, TQ35_04470
GN   {ECO:0000313|EMBL:KJR78972.1};
OS   Candidatus Aramenus sulfurataquae.
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Candidatus Aramenus.
OX   NCBI_TaxID=1326980 {ECO:0000313|EMBL:EWG06998.1, ECO:0000313|Proteomes:UP000054284};
RN   [1] {ECO:0000313|EMBL:EWG06998.1, ECO:0000313|Proteomes:UP000054284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1-illumnia {ECO:0000313|EMBL:EWG06998.1};
RX   PubMed=24604657;
RA   Servin-Garciduenas L.E., Martinez-Romero E.;
RT   "Draft Genome Sequence of the Sulfolobales Archaeon AZ1, Obtained through
RT   Metagenomic Analysis of a Mexican Hot Spring.";
RL   Genome Announc. 2:e00164-14(2014).
RN   [2] {ECO:0000313|EMBL:KJR78972.1, ECO:0000313|Proteomes:UP000053480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1-454 {ECO:0000313|EMBL:KJR78972.1};
RA   Servin-Garciduenas L.E., Martinez-Romero E.;
RT   "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT   Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000256|HAMAP-Rule:MF_00712}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00033655, ECO:0000256|HAMAP-
CC         Rule:MF_00712};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00712}.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00712}.
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:EWG06998.1}.
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DR   EMBL; ASRH01000005; EWG06998.1; -; Genomic_DNA.
DR   EMBL; JZWS01000032; KJR78972.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7KLB3; -.
DR   PATRIC; fig|1326980.6.peg.1137; -.
DR   Proteomes; UP000053480; Unassembled WGS sequence.
DR   Proteomes; UP000054284; Unassembled WGS sequence.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 1.
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   HAMAP; MF_00712; GcvPA; 1.
DR   InterPro; IPR023010; GcvPA.
DR   InterPro; IPR049315; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42806; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1.
DR   PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   PIRSF; PIRSF006815; GcvPA; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00712}; Reference proteome {ECO:0000313|Proteomes:UP000054284}.
FT   DOMAIN          12..417
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
SQ   SEQUENCE   453 AA;  50664 MW;  CDB69AEAFAC39CC4 CRC64;
     MEMHPWLPNL GDLREMLKEI GVKDVEELFS DIPKEIVLKR ELNVGYGRPL SEYEIARRLE
     ELSEMNAKLL YPPFLGGGVC PHYVPYAVKM IISRSEFYTA YTPYQPEANQ GLLQALFEYQ
     SYMAELLQME VVNSSLYDWG GALAEAILMV NRINGKKKVI VPTNANPNHL KVAETWVKGK
     GIELVKVKYN EEGKIDVEDL EKKLTDDIGA VYLQTPNFFG VFETEVEGVV ELARKKGALT
     IMGVNPLALA LIKPPGEYNV DIAIGDAQEL GIPLSMGGPS LGVFATRWDA KLVRQMPGRI
     VGLTKDSFGK EGFTLILQTR EQFARREKAT SNITTNEALM AIAVAVYLSL LGRNGLKELA
     EEVYLRSHYA TKLVESRGIG KRKFLGDFFE EVTLTFPVEY QRIHEKLLKA GLHGGLGIDD
     YSAVFCFTEV HPKKAIDLLV EKVEEVVKNV EAS
//
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