ID A0A419S947_9SPHI Unreviewed; 961 AA.
AC A0A419S947;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=BCY91_16095 {ECO:0000313|EMBL:RKD18321.1};
OS Pelobium manganitolerans.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pelobium.
OX NCBI_TaxID=1842495 {ECO:0000313|EMBL:RKD18321.1, ECO:0000313|Proteomes:UP000283433};
RN [1] {ECO:0000313|EMBL:RKD18321.1, ECO:0000313|Proteomes:UP000283433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YS-25 {ECO:0000313|EMBL:RKD18321.1,
RC ECO:0000313|Proteomes:UP000283433};
RA Wu S., Wang G.;
RT "Genome of Pelobium manganitolerans.";
RL Submitted (JUL-2016) 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|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
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:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
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:RKD18321.1}.
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DR EMBL; MBTA01000005; RKD18321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419S947; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000283433; 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 CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR049316; GDC-P_C.
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 NCBIfam; TIGR00461; gcvP; 1.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000283433}.
FT DOMAIN 14..437
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 442..737
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..898
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 961 AA; 105837 MW; C8026CBF727EB0DB CRC64;
MKLNVFYKEA FETRHIAPDL QNTQAMLKSI GADSLDALIN QTVPENIRLK QALNLPEPKS
EFEYLNKLRQ TASKNKVYKS YIGQGYYDVI VPAVIQRNVL ENPGWYTQYT PYQAEISQGR
LQALLNFQTM VIDLTGMEIA NASLLDEGTA AAEAMFMQYS LRKNQNAKSY FVSEEVFPQT
IDILKTRAQP YGITLIIGNH QTAELNEDFF GALVQYPAGQ GAVYNYGEFA TAAHEKDIKL
TVVADLMSLA LLSPPGEWGA DIVVGTTQRF GVPMGFGGPH AAYFATKEVY KRSMPGRLIG
VTIDAHNNYA LRMALQTREQ HIRRDKATSN ICTAQALLAI MAGMYATYHG PQGIKAIAQR
IHGMAVLLSK ALAQFGYQQL NESYFDTLKF SVGDLVNPIH SEALNNQFNL NYDGDIITIA
LDETTRLHDI ETIVKVFGKV KAKTLNDIDI YALAEEVEST IPVSQQRTSD FLTHPVFNTH
HSEHEMLRYI KSLEAKDLSL CHSMIPLGSC TMKLNATTEM IPVTWPEFSS LHPFSPADQT
GGYMQIMAEL NTWLAEITGF AAMSLQPNAG AQGEYAGLMV IRAYHHDRGE QHRNVVLIPS
SAHGTNPASA AMAGMKIVVT KCDERGNIDV ADLRAKAEEH AANLSCLMVT YPSTHGVFEE
SIIEICDIIH KHGAQVYMDG ANMNAQVGLT SPATIGADVC HLNLHKTFCI PHGGGGPGMG
PIGVASHLVP YLPGHSVVDI NHEKSIHAVS AAPWGSASIL LISHAYVAMM GTKGLTRATQ
FAILNANYIK SRLEQHYPVL YAGANGRCAH EMILDCRGFK NFGIEVTDVA KRLMDYGFHA
PTVSFPVAGT LMVEPTESEP KEELDRFCDA MIAIRAEIRA VEEALIDGKN NPLKNAPHTM
SAVTASDWDK PYSREQAAFA LPYLKQNKFW PSVGRVNDTF GDRTLICSCP PVTDYEFDVL
V
//
