ID A0A1H2HNI4_9PSED Unreviewed; 956 AA.
AC A0A1H2HNI4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05216296_3142 {ECO:0000313|EMBL:SDU33407.1};
OS Pseudomonas pohangensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=364197 {ECO:0000313|EMBL:SDU33407.1, ECO:0000313|Proteomes:UP000243232};
RN [1] {ECO:0000313|Proteomes:UP000243232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17875 {ECO:0000313|Proteomes:UP000243232};
RA Varghese N., Submissions S.;
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; LT629785; SDU33407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2HNI4; -.
DR STRING; 364197.SAMN05216296_3142; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000243232; Chromosome i.
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; 1.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 1.
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:UP000243232}.
FT DOMAIN 18..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..899
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 956 AA; 103294 MW; 15735C4A8E1DB0B9 CRC64;
MSQSPSLAQL QSEAFLGRHL GPDAVEQQSM LSSLAVATRA ELIAQTVPPA IRLNGPLGLP
AALDEEGALA KLRGYAAQNE VWTSLIGMGY HGTLTPTVIL RNVLENPGWY TAYTPYQPEI
AQGRLEALLN FQQLTIDLTG LDLASASLLD EATAAAEAMA MAKRVAKSKS NLFFVDQNCH
PQTISVVQTR AEAFGFELAI DSVDNLANYQ VFGGLLQYPD SQGEIRDIKP LIDQLHAQQA
LACVSADILG LLLLTPPGEL GADVVFGSAQ RFGVPMGYGG PHAAFFACRD EYKRAIPGRI
IGVSKDARGN SALRLALQTR EQHIRREKAN SNICTSQVLL ANIASLYAVY HGPQGLKRIA
QRVQRLTAIL AAGLEQKGFK RLNNHFFDTL TVQVGNQQAA ILARAHIQCI NLRVIGEDVL
AVSLDETCSA DTVANLFDLF LGEEHGLDVA ALDAAGVASG IPAGLERSSA YLTHPVFNSH
HSETEMLRYL KQLETKDLAL NTAMIPLGSC TMKLNATSEM IPITWPQFAN LHPFVPVEQA
EGYRLMIEEL ESWLCAITGF DAICMQPNSG AQGEYAGLLA IRKYHESRGD AHRNICLIPA
SAHGTNPASA QMASMRVQIV ACDDEGNVDL ADLKKKAAEA GEQLACLMAT YPSTHGVYEE
GIREICEVIH SHGGQVYMDG ANLNAQVGLT RPADIGADVS HMNLHKTFCI PHGGGGPGMG
PIGVKAHLAP FVANHPVVPI KGPNPGNGAV SAAPWGSASI LPISWMYIAM MGPQLADATE
VAILNANYLA KALGEAFPVL YAGRNGRVAH ECILDLRPLK AETGISEEDV AKRLMDYGFH
APTMSFPVPG TLMIEPTESE SKHELDRFIE AMLSIRAEIA KVQEGQWPAE DNPLKRAPHT
LADVIGVWER PYSIEHAVSP TTHTRLHKYW PTVNRVDNVY GDRNLFCACV PLSDYQ
//
