ID A0A1H8YH10_9PSEU Unreviewed; 963 AA.
AC A0A1H8YH10;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN04489732_11678 {ECO:0000313|EMBL:SEP51504.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEP51504.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEP51504.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEP51504.1,
RC ECO:0000313|Proteomes:UP000198582};
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:ARBA00033655, 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; FOEF01000016; SEP51504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8YH10; -.
DR STRING; 394193.SAMN04489732_11678; -.
DR Proteomes; UP000198582; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198582}.
FT DOMAIN 29..454
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 485..738
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 784..905
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 963 AA; 102010 MW; CC7FBFC98A736ABA CRC64;
MTEGEFPVHR CARCPSRGAP ITSTPFDARH IGPAEAERAK MLAETGHGSL DSLVEAAVPS
AIRATRDLDL PAAATEEEAT AELRALAALN RPMTQMIGLG YSDTVTPGVI RRNVLENPAW
YTAYTPYQPE ISQGRLEALL NFQTMVADLT GLATANASLL DESTAVAEAM TLMRRASKAK
SNVVVLDAEC LPQTIAVVRT RAAALGIDVQ VRDLLTGLPE EFFGMVVQYP GASGVLRGRG
FYHAVSEAAK AAGALYTVAA DLLALTLITS PGEFGADVAA GSTQRFGVPL GYGGPHAGYM
AVRAGLERSL PGRLVGVSVD ADGNSAYRLA LQTREQHIRR EKATSNICTA QVLPAVLAAM
YAVYHGPDGL QAIANRVHGL AAGLADALRA GGVEVVHESF FDTVVAHVPG RAAEVHEAAR
EAGINLGHVD ADHVRVACDE VTRPDTIAKV LRAFGVDAKW TVATALPNGI VRESGFMGHE
VFSTHRSETA MLRYLRRLSD QDYALDRGMI PLGSCTMKLN ATTEMEPISW REFAGIHPFA
PAEDAQGYHV LVEQLSGWLA EVTGYDRVSL QPNAGSQGEL AGLLAIRGYH HANGQPERDV
CLIPSSAHGT NAASAVLAGM RVVVVKCTDE GNVDLADLQA KVDAHRETLA AIMVTYPSTH
GVYEHGIERL AKIVHDGGGQ VYVDGANLNA LLGLAKPGEF GGDVSHLNLH KTFCIPHGGG
GPGVGPVAVR AHLAPYLPNH PLLDQAGPAT GVGPISGAPY GSASILPISW AYVRMMGGPG
LTTATKVAVL AANYVASRLS PHFPVLYTGQ DGLVAHECIL DLRGITKETG VTVDDVAKRL
IDYGFHAPTM SFPVAGTLMV EPTESEDLGE IDRFIAAMIA IRGEIDQVAA GRWTAETSPL
RGAPHTAEAL VGEWDADYDR ELAVYPAGVS RKNKYWPPVR RIDGARGDRN LVCSCPPLNA
YEG
//