ID A0A2L2BPE8_9MICO Unreviewed; 982 AA.
AC A0A2L2BPE8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=C3B54_11551 {ECO:0000313|EMBL:AVG23539.1};
OS Pontimonas salivibrio.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Pontimonas.
OX NCBI_TaxID=1159327 {ECO:0000313|EMBL:AVG23539.1, ECO:0000313|Proteomes:UP000243077};
RN [1] {ECO:0000313|EMBL:AVG23539.1, ECO:0000313|Proteomes:UP000243077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL-TW6 {ECO:0000313|EMBL:AVG23539.1,
RC ECO:0000313|Proteomes:UP000243077};
RA Cho B.C., Hardies S.C., Jang G.I., Hwang C.Y.;
RT "Complete genome of the streamlined marine actinobacterium Pontimonas
RT salivibrio CL-TW6 adapted to coastal planktonic lifestype.";
RL Submitted (FEB-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}.
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DR EMBL; CP026923; AVG23539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2BPE8; -.
DR KEGG; psai:C3B54_11551; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000243077; 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; 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:UP000243077}.
FT DOMAIN 9..421
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 455..728
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 MOD_RES 699
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 982 AA; 104709 MW; 8895CE08F8BD4E23 CRC64;
MTQQPFSARH LGVDDSAEAL MLQALGFESL DELMDKAVPA HLSQGALESI IPPPASEAEV
LQELRALADH NNAHRSMLGM GYYPSYTPSV VKRNVFENPS WYTAYTPYQP EISQGRLEAL
LNFQTMVGDL TGLPVANASM LDEATAVAEA MLLARRASGV AANVFLVDVD TLPQTKAVLA
GRAEPLGIEL EETDFSGELP EAFGAIVQYP GASGRVWDPR GAISRVKDAG GLAVVAADLM
ALTLLTPPGE MSADIAVGTT QRFGIPLGFG GPHAGYLAVR AGLERQMPGR LVGVSQDRFG
NPAYRLTLQT REQHIRRDRA TSNICTAQVL LAVMAGMFAV YHGPDGLRSI ATSIAAQAAG
FAKRLKEAGF DLVHDEFFDT IQVRTPGKAH DIVQTAYTHG LLIRAVDSDT VSLSFDQTTA
EASGRGVGAD VFEALSVAFG LTGYRGQHAE DNALPAGLKR TTSYLDHPVF HVHQSETQMM
RYLKSLADKD YALDRGMIPL GSCTMKLNAA TEMEAVSWPE FAGLHPFAPA DDVAGYMVLM
SHLETWLAEL TGYDSVSLQP NAGSQGEYAG LLAIRGYHRS RGDHHRTICL IPSSAHGTNA
ASAVLAGMQV VVLACNEQGD VDIDDVKAKI AEHGENLAAL MVTYPSTHGV YEHGINTITD
LVHEAGGQVY IDGANLNALV GFSRYGDIGG DVSHLNLHKT FCIPHGGGGP GVGPVGAKAH
LAPFLPGHPF AQTTAHPPFD EGSGQTGSFV HQGPAVSAAP YGSPSILPIS WAYVRMMGPE
GLRKATARAV LAANYIASRL AEHYPVLYVG ENGLVAHEVV LDIRPITAET GVSVDDVAKR
LMDYGFHAPT MSFPVPGTLM VEPTESEDLG ELDRFIDAMI RIREESRAVK DGVWPAEDNP
LTNAPHPAAE AISDLWEHPY SRTLATYPAI GGVDSSQHGA DPRVISKYWM PVGRVDQAYG
DRNLVCACPP IEAFAGAGVS PG
//
