ID A0A0M4RCK4_9MICC Unreviewed; 964 AA.
AC A0A0M4RCK4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AOC05_12275 {ECO:0000313|EMBL:ALE92893.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE92893.1, ECO:0000313|Proteomes:UP000062833};
RN [1] {ECO:0000313|Proteomes:UP000062833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Arthrobacter alpinus strain R3.8.";
RL Submitted (SEP-2015) 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; CP012677; ALE92893.1; -; Genomic_DNA.
DR RefSeq; WP_062007473.1; NZ_CP012677.1.
DR AlphaFoldDB; A0A0M4RCK4; -.
DR KEGG; aaq:AOC05_12275; -.
DR PATRIC; fig|656366.3.peg.2654; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000062833; Chromosome.
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:UP000062833}.
FT DOMAIN 12..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 478..739
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 780..901
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 703
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 101571 MW; 88BB24C0E92B7F4E CRC64;
MTIQSIPTVF ADRHIGARRQ LDIAHMLKAI GYDSVDSLVD TAVPDSIRQG TPLKLQGALS
EVEVLAELRA LAAKNKRAIQ MIGQGYYDTV TPAVIRRNIL EGPAWYTAYT PYQPEISQGR
LEALLNFQTM VSDLTALPVA NASLLDEATA VAEAVLLMRR ANKSKTAANG KTVLDADLLP
QTIALVKGRA EALGFEVEVA DLSLGLPDGD INGVVLQQPG VSGRVFNHAP VITAAKERGA
LVTVAADLLA LTLITPPGEQ DADIAVGTAQ RFGVPLFFGG PHAAYMAVRN GMERSLPGRI
VGVSKDDTGL PAYRLALQTR EQHIRREKAT SNICTAQALL AIVASMYAVY HGPEGLKAIA
ETVHGHARTL AAALAASGVE LLHTSFFDTL TVHVPGRAGT LVAAAERAGI NLRPIDANTV
GISIDETTTA DIVARVAAVF GAAPAGDGAD QAGAAFALAA DTERTSDFLT HPVFNTHRSE
TQLLRYIRRL SDRDLALDRT MIPLGSCTMK LNATAEMEAI SWPEFASIHP FAPDSQTIGW
RELIEGLEAD LCEITGYDQV SIQPNAGSQG ELAGLLAIRG YHISRGDAQR TVCLIPGSAH
GTNAASAVLA GMKVVVVATA TDGSIDHADL LTKIDTHKDQ LSAIMITYPS THGVYDADVR
EVCDAVHAAG GQVYVDGANL NALVGLAQPG KFGGDVSHLN LHKTFCIPHG GGGPGVGPVA
AKAHLAPFMP GDANAAANDA SQGTPSSGVP ISGSRFGSAG VLPISWAYVK LMGGNGLTEA
TKSALLAANY IAARLNEHFP VLYTGAGDLV AHECILDLRE LTAKTGVTAE DVAKRLIDYG
FHAPTLSFPV SGTLMVEPTE SEDLTEINRF ITAMVSIRAE IDQVAEGVFT LEDSPLRNAP
HTAAAVVNSA WERGYTREQA AFPVAALRQD KYFPPVGRID GAAGDRNLVC SCPPIEDFAD
DFSN
//
