ID A0A1G9LKX5_9ACTN Unreviewed; 943 AA.
AC A0A1G9LKX5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05421874_12547 {ECO:0000313|EMBL:SDL62504.1};
OS Nonomuraea maritima.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=683260 {ECO:0000313|EMBL:SDL62504.1, ECO:0000313|Proteomes:UP000198683};
RN [1] {ECO:0000313|EMBL:SDL62504.1, ECO:0000313|Proteomes:UP000198683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDL62504.1,
RC ECO:0000313|Proteomes:UP000198683};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNFB01000025; SDL62504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9LKX5; -.
DR STRING; 683260.SAMN05421874_12547; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000198683; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198683}.
FT DOMAIN 12..433
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 465..722
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 763..884
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 694
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 943 AA; 100266 MW; 7B8C1E4C1A16D818 CRC64;
MTDLSAPPFS TRHIGPSESE QQRMLEAVGF ESVADLVAVA VPEAIRAKDS LQLPAPVGEA
EAIGELRALA GRNRVMTSMI GLGYYDTVTP AVIRRNLLEN PGWYTAYTPY QPEISQGRLE
ALLNFQTVVS DLTGLPVAGA SLLDEGTAAA EAMTLARRAG KSKSSVFVVD ADALPQTKAV
LATRAEPLGI TLVEHDLEGD LPECFGVLVQ YPGASGWVRD FRAVAAAAHE AGALVVAAAD
LLALTLVAAP GELGADIAIG SSQRFGVPFG FGGPHAAYMS VQEGLQRQLP GRLVGVSVDA
DGGPAYRLAL QTREQHIRRE KATSNICTAQ VLLAVIAGMY AVYHGPEGLR RIAHRVHRHA
VVLADGLRGA GVEVEHGEFF DTVLARVPGR AAEIVAAAAE QGVNLWQADA DHVAISCDEK
TGAAEVAKVW AAFGVPAGEV DVEGAADALP QSLARESGYL THPVFHQHRS ETAMLRYLRK
LQDKDIALDR SMIPLGSCTM KLNATTEMEP ITWPEFAAIH PYAPEEQSEG YRELIGSLES
WLAEVTGYDA VSIQPNAGSQ GEFAGLLAIR AYHRASGHGE RDVCLIPSSA HGTNAASAVM
AGMRVVVVAC DDQGNVDLAD LDAKIDKHRD ALAAIMVTYP STHGVYEETI TEICEKVHAA
GGQVYVDGAN LNALVGLAKP GAFGADVSHL NLHKTFCIPH GGGGPGVGPV AVRAHLAEFL
PGHPLRDGSA VGPVSAAPYG SAGILPISWA YVRMMGAEGL KSATEQAILS ANYVARRLAP
HYPVLYTGRG GLVAHECIID LRQITKETGV TVDDVAKRLI DYGFHAPTMS FPVAGTLMIE
PTESEDLREL DRFVDAMIAI RGEIAKVASG DYDKTDNPLR NAPHTAEAVT ADDWSHPYTR
AEAAYPVPSL RDGKYWVPVR RIDQAYGDRN LVCSCPPLEA YED
//
