ID A0A1H1A8D9_9ACTN Unreviewed; 964 AA.
AC A0A1H1A8D9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN04489718_1452 {ECO:0000313|EMBL:SDQ35606.1};
OS Actinopolyspora saharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=995062 {ECO:0000313|EMBL:SDQ35606.1, ECO:0000313|Proteomes:UP000199301};
RN [1] {ECO:0000313|EMBL:SDQ35606.1, ECO:0000313|Proteomes:UP000199301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45459 {ECO:0000313|EMBL:SDQ35606.1,
RC ECO:0000313|Proteomes:UP000199301};
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; FNKO01000001; SDQ35606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1A8D9; -.
DR STRING; 995062.SAMN04489718_1452; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000199301; 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}.
FT DOMAIN 19..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 457..739
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 786..907
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 713
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 104024 MW; FF48ED2A91C32B1B CRC64;
MTDDRIPLAA LEHGTPFAER HVGPMPAELA SMLDVVGVGS LEELGEHAVP AGIRERDSQL
RLPEPATEAE SLDELGELAS RNTPHVEMIG LGYHATVTPP VIRRNVLENP AWYTAYTPYQ
PEISQGRLEA LLNFQTMVAD LTGVPVSNAS MLDESTAAAE GMTLIRRAGR AKSPRFVVDD
DAFPQTLSVI ETRAEPLGIE IVRADLSRGV EGLPEGDFFG ALLAYPGASG AVRDHEEVIA
EIHRRGGMAV VSADLLALTM LRAPGEMGAD VVVGTTQRFG VPMGFGGPHA GYMAVRKGVE
RQLPGRLVGV SVDADGNQAY RLALQTREQH IRREKATSNI CTAQVLLAVV ASMYAVYHGP
AGLRSIATRT HRMATVLAEQ LRRGGVRVCH DEFFDTVLTR VPGRADEIVA AARRNGVNLR
RVDADHVGIT CDETTTRDRL ALVWRAFGLE EGERTPVDEL DAEVGRALPE GLLRESDYMT
HPVFHRHRSE TALLRYLRRL SDSDVALDRS MIPLGSCTMK LNAAAEMEPI TWPSIAELHP
FAPAEDAAGL LRVVEDLQDW LAEITGYDAV SLQPNAGSQG EFAGLLAIRA YHRERGQGQR
EVCLIPASAH GTNAASAVMA GLRVVVVRCD DEGNIEMDHL RELVDKHQDD LAAIMITYPS
THGVYEDTVQ EVCGVVHEAG GQVYVDGANL NALIGLARMG KFGADVSHLN LHKTFCIPHG
GGGPGVGPIG VREHLSPFLP NHPLQPQAGP ETGVGPISAA PWGSASILPI SWAYVRMMGA
DGLRRATLTA VASANYVASR LNDHFPVLYT GNGGFVAHEC ILDLREVTKN AGLSVDDVAK
RLADYGLHAP TMSFPVAGTL MVEPTESENL EELDRFCDAM IAIRAEIDKV AAGAWPAEDN
PLVNAPHTAA ALAGDWEHSY GRWEAVYPMG TPENKIWPPV RRIDQAHGDR NLVCSCPPLS
AYEG
//
