ID A0A410UQZ1_9BURK Unreviewed; 959 AA.
AC A0A410UQZ1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ECO:0000313|EMBL:QAU33746.1};
GN ORFNames=EKL02_05860 {ECO:0000313|EMBL:QAU33746.1};
OS Janthinobacterium sp. 17J80-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2497863 {ECO:0000313|EMBL:QAU33746.1, ECO:0000313|Proteomes:UP000288813};
RN [1] {ECO:0000313|EMBL:QAU33746.1, ECO:0000313|Proteomes:UP000288813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17J80-10 {ECO:0000313|EMBL:QAU33746.1,
RC ECO:0000313|Proteomes:UP000288813};
RA Kim M., Maeng S., Sathiyaraj S.;
RT "genome sequence of Janthinobacteria sp. 17J80-10.";
RL Submitted (JAN-2019) 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; CP035311; QAU33746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410UQZ1; -.
DR KEGG; jaj:EKL02_05860; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000288813; 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:UP000288813}.
FT DOMAIN 18..442
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 453..735
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 707
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 959 AA; 103242 MW; 249DC1EE33EB1E90 CRC64;
MTNASLTQLE AHDAFIARHI GPSEAEQAAM LAVLGYPNRT ALIDAIVPDN IRRRDVLPLG
EFTKAQSEPE ALAQLKALAG KNKVLKSLIG QGYYNTHTPG VILRNVFENP AWYTAYTPYQ
PEISQGRLEA MLNFQQMITD LTGMDIANAS MLDEGTAAAE AMTLIQRVGK STSSVFYVAA
DVLPQTREVI ETRAKPLGVE VRTCDGKAEL EGECFGVLLQ YPGVNGDIRD YREYASAMHA
KGTMVIVAAD LLALTLITPP GEWGADVVVG NSQRFGVPLG FGGPHAGYMS TRDAFKRNMP
GRLVGVTIDA QGNQAYRLAL QTREQHIRRE KATSNICTAQ VLLAVIASMY AVYHGPEGLR
RIAQRVHRFT GILAAGLTHL GYKLANTTYF DTLTINVSDA AALHTAAEAA GINLRQISAT
QVGISLDETI TREDIATLWT IFAQGKATPD FAAIDAGVDD ALPKALARTS AYLTHPTFSR
YHAEHEMLRY LRSLADKDLA LDRTMIPLGS CTMKLNATSE MIPVTWPEFS NIHPFAPADQ
TVGYREMIDQ LEAMMCAATG YAAVSLQPNA GSQGEYAGLL VIQAYHASRG EAHRNICLIP
SSAHGTNPAS ASMVGMEVVV VACDERGNVD LADLKAKAEK HSANLAAVMV TYPSTHGVFE
EGIQSLCEIV HAHGGQVYVD GANLNAMVGV AAPGKFGGDV SHLNLHKTFC IPHGGGGPGV
GPVAVGAHLA QFLPNQKSTG YTRSEQGIGA VSAAPFGSAS ILPISWMYVA MMGAEGLKAA
TETAILAANY IARRLAPHYP VLYSGHDGLV AHECILDLRP ITDATGISNE DVAKRLIDFG
FHAPTMSFPV PGTLMIEPTE SESQAELDRF IDAMIAIRME IAKVASGEFD ARDNPLKNAP
HTVQVMVADK WEHAYSREVA AYPVASLRQQ KYWSPVGRAD NVYGDRNLFC SCVPMSDYE
//
