ID A0A1H8T5B2_9ACTN Unreviewed; 998 AA.
AC A0A1H8T5B2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05660991_02076 {ECO:0000313|EMBL:SEO86082.1};
OS Trujillella endophytica.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Trujillonella.
OX NCBI_TaxID=673521 {ECO:0000313|EMBL:SEO86082.1, ECO:0000313|Proteomes:UP000198960};
RN [1] {ECO:0000313|EMBL:SEO86082.1, ECO:0000313|Proteomes:UP000198960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45413 {ECO:0000313|EMBL:SEO86082.1,
RC ECO:0000313|Proteomes:UP000198960};
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; FOEE01000005; SEO86082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8T5B2; -.
DR STRING; 673521.SAMN05660991_02076; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000198960; 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 24..448
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 486..744
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 785..906
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 958..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 715
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 998 AA; 104649 MW; 6EEBCB6243765F73 CRC64;
MADAAPGPLP TLRALSPAGS FAARHIGPRP AETAEMLATI GHDSLRSLVD ATVPEGVRDR
RPLDLPAAAD ESAVLAALRE RAEANEVFSS MIGLGYSGTV TPAVIQRVIL ENPAWYTAYT
PYQPEISQGR LEALLNFQTM VADLTGLPVA GASMLDEATA AAEAMTLVRR AGRAKADAVF
VVDADTLPQT LAVLRTRAEP LGIGLHVADL SGGWPDDLPE AGAFGVLLSF PGAGGAVRDH
RALAAAAHEA GAAVVVAADL LALTLLEAPG EWGADVACGS TQRFGVPLGF GGPHAGYLSV
REGLARQLPG RLVGVSVDAD GAVAYRLALQ TREQHIRREK ATSNICTAQV LLAVMAGAYA
VYHGPDGLTA IAARVHRSAV VLAGWLRAGG LEVAHEAFFD TLTVAVPGRA ADVVAAAAQR
RINLRLVDAD TVAVACDETT TPEILALVAE AFGVPGDPDA ARDDDGADAL PAGLRRRTPF
LTHPVFSAHR SETALMRYLR SLSDKDLALD RTMIPLGSCT MKLNSAVEMA AITWPEFAGI
HPFAPAGQTA GYRRLIDELC EGLAEITGYA AVSVQPNAGS QGEFAGLMAI RGYHHARGEA
FRDVCLIPSS AHGTNAASAV MAGMRVVVVA CDEAGNVDLA DLRAKVERHA DRLAAIMITY
PSTHGVFETE VQEICAAVHD AGGQVYVDGA NLNAMVGLAR PGRFGSDVSH LNLHKTFCIP
HGGGGPGVGP IGVREHLVPF LPGHPLVDTG AQGPAVSAAP WGSAGILPIS WAYLRLMGPD
GLQRATEHAI LGANYLAARL REHFPVLYTG RDGLVAHECI LDIRPLTKAT GVTNDDIAKR
LVDFGFHAPT MSFPVAGTLM VEPTESEDKR ELDRFVEAMV AIRAEIDKVA SGEYDREDNP
LRNAPHTLAM VAGEWGRPYP RSTAVYPVPG LAGRGYLSPV RRIDQAYGDR NLVCSCPSPE
AFAEPEPPSA PVGRVPGRGE GAPDDLGTTE DVVGAARA
//
