ID A0A366ZN87_9ACTN Unreviewed; 1008 AA.
AC A0A366ZN87;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:RBY78754.1};
GN ORFNames=DQ238_11860 {ECO:0000313|EMBL:RBY78754.1};
OS Geodermatophilus sp. TF02-6.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY78754.1, ECO:0000313|Proteomes:UP000253027};
RN [1] {ECO:0000313|EMBL:RBY78754.1, ECO:0000313|Proteomes:UP000253027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-6 {ECO:0000313|EMBL:RBY78754.1,
RC ECO:0000313|Proteomes:UP000253027};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL Submitted (JUL-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:RBY78754.1}.
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DR EMBL; QOHF01000011; RBY78754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366ZN87; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000253027; 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:UP000253027}.
FT DOMAIN 32..461
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 495..753
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 794..915
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 967..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 724
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1008 AA; 105840 MW; 9FB1D6409CD859EF CRC64;
MSAGSLPVVV DRGRDALPAL SSLDPAGSFA GRHIGPRPEQ TAAMLAAVGH PTLQSLVDAC
VPEGVRDRAP LDLPPAADEA TVLRLLRERA AANDVYTSMI GLGYSATVTP AVIQRAVLEN
PAWYTAYTPY QPEISQGRLE ALLTFQTVVA DLTGLPVAGA SMLDEATAAA EAMTLVRRAG
RRGGDDPAVF VVDADTLPQT LAVLHTRAEP QGIRLHVADL SAGWPADLPE AGAFGVLLSY
PGASGAVRDH RALAAAAHRA GAAVVVAADL LALTLLEAPG EWGADVACGS SQRFGVPMGY
GGPHAGYLSV REGLARQLPG RLVGVSVDAD GDVAYRLALQ TREQHIRREK ATSNICTAQV
LLAVMAGAYA VYHGAEGLTA IAARVHRGAQ ALAAWLRAGG VQVVHDRFFD TVQARVPGRA
AEVVAAAAAR RINLRRVDDD TVGVACDETT TVDTLRAVAE AFGVPVDVAV LDDDGADALA
PELRRRTPFL THPVFAAHRS ETALLRHLRS LADKDLALDR TMIPLGSCTM KLNSAVEMAA
ITWPEFAQLH PFAPAEQARG YRQLIDELCT ALAEVTGYAA VSVQPNAGSQ GEFAGLLAIR
GYHRSRGEEQ RDVCLIPSSA HGTNAASAVM AGMRVVVVAC DEAGNVDVDD LQRKVDQHAE
RLAAVMITYP STHGVFETGI GEVCAAVHDA GGQVYVDGAN LNAMVGLARP GRFGSDVSHL
NLHKTFCIPH GGGGPGVGPI GVAAHLVPFL PGHPVVDTGA SGPTVSAAPW GSAGILPISW
AYLRLMGPDG LTLATEHAIL AANYLATRLR EHYPVLYTGA DGLVAHECIL DVRPLTKATG
ITNDDIAKRL IDYGFHAPTM SFPVAGTLMV EPTESEDVGE LDRFVDAMVA IRGEIEKVAT
GEYDRTDNPL RNAPHTLAMV VGEWDRPYPR EVAVYPLPAL RGRGYLPPVR RIDQAHGDRN
LVCSCPPPEA FAEPEPAPGP VARLPSRVEG APDDLGTAAD AVPAGAQA
//
