ID A0A3A5MII6_9MICO Unreviewed; 982 AA.
AC A0A3A5MII6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:RJT86828.1};
GN ORFNames=D6T64_16945 {ECO:0000313|EMBL:RJT86828.1};
OS Cryobacterium melibiosiphilum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=995039 {ECO:0000313|EMBL:RJT86828.1, ECO:0000313|Proteomes:UP000272015};
RN [1] {ECO:0000313|EMBL:RJT86828.1, ECO:0000313|Proteomes:UP000272015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hh39 {ECO:0000313|EMBL:RJT86828.1,
RC ECO:0000313|Proteomes:UP000272015};
RA Liu Q., Xin Y.-H.;
RT "Novel species of Cryobacterium.";
RL Submitted (SEP-2018) 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:RJT86828.1}.
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DR EMBL; QZVS01000093; RJT86828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5MII6; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000272015; 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; 1.
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}.
FT DOMAIN 22..454
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 488..747
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 803..924
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 717
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 982 AA; 103809 MW; 4E83637A90F3E544 CRC64;
MTSSTTPAVR TSPAPAALPF VERHIGTDAA AQQHMLATLG YDSLDALVDA AIPANIHADS
FRTAGDSTLP PAATEREAIA ELRVMAEWNT VKRSMIGLGY YDTITPAVIQ RGVFENPSWY
TAYTPYQPEI SQGRLEALIN FQTMIADLTG LSTANASMLD ESTAVVEGML LARRASKVAA
RRFIVDADAF PQTHALLANR AAALGIELAI VDLNEQTTAA DLGEYFGVFV QYPSKSGRVW
NPASVIALAH EQKALAVVAA DLLALTLITS PGELGADVAV GTSQRFGVPM GFGGPHAGYM
AVRGGLERQL PGRLVGVSVD AAGHPAYRLA LQVREQHIRR DKATSNICTA QVLLAVMAGM
YAVYHGPDGL RQIAGQVHEK AGQLAAALTA AGAEVLSTSF FDTLLVSVPG RAEEILARAA
ENDVNLRLVD GDTLGLSVDE TTTLADLSWV VQAFGGSDAF GHVDFGTAVV GLPAELARTS
EFLTHPVFNT HRSETSMMRY LKRLADADYA LDRGMIPLGS CTMKLNAASE MAAVSWPEFA
GLHPFAPRAD VEGYLGLVRQ LETWLTDVTG YDSVSLQPNA GSQGELAGLL AIAGYHRSRG
DTARTVCLIP SSAHGTNAAS AALAGMRVVV VACDELGNVD LDDLTAKIVE HTADLAALMI
TYPSTHGVYE HEVATICRAV HDAGGQVYVD GANLNALLGF ARYGDFGGDV SHLNLHKTFC
IPHGGGGPGV GPVAAKAHLA AFLPGHPLAQ SDEHYLLTPP DEPTATVVHG GGPVSAAPYG
SPSILPISWA YVRMMGADGL RAATGAAVLA ANYVARRLEG AYPLLYSGEN SLVAHECILD
LRPLTAATGV TVDDVAKRLI DYGFHSPTMS FPVAGTLMVE PTESEDLAEI DRFIEAMLAI
KAEADAVAAG TWPADDNPLH NAPHTAQAVI AGEWEHPYDR ETAVYPLASL VRGKYWPPVR
RIDNAFGDRN LACSCPPPEA FE
//
