ID A0A3P1SXE0_9GAMM Unreviewed; 968 AA.
AC A0A3P1SXE0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-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:RRD01718.1};
GN ORFNames=EHS89_03975 {ECO:0000313|EMBL:RRD01718.1};
OS Amphritea balenae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Amphritea.
OX NCBI_TaxID=452629 {ECO:0000313|EMBL:RRD01718.1, ECO:0000313|Proteomes:UP000267535};
RN [1] {ECO:0000313|EMBL:RRD01718.1, ECO:0000313|Proteomes:UP000267535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAMM 1525 {ECO:0000313|EMBL:RRD01718.1,
RC ECO:0000313|Proteomes:UP000267535};
RA Fang Z., Zhang Y., Han X.;
RT "The draft genome sequence of Amphritea balenae JAMM 1525T.";
RL Submitted (NOV-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: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRD01718.1}.
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DR EMBL; RQXV01000001; RRD01718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1SXE0; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000267535; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
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; PF01212; Beta_elim_lyase; 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}.
FT DOMAIN 21..444
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 546..699
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT DOMAIN 787..908
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 714
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 968 AA; 105197 MW; 9C8DAEA79CADEA79 CRC64;
MSADNTLSLA QLEQTDAFIG RHIGPNAAEQ QAMLAELGLE SLDQLIEQTV PESIQLAQPI
DLADSRTEED VLSELKQIAS KNVINRSMIG MGYSDTIVPN VILRNVLENP GWYTAYTPYQ
PEVAQGRLEA LLNYQQMVLD LTGLDLANAS LLDESTAAAE AMTLCKRMSK ARKANIFLVD
ENLHPQNISV IETRAEPLGY EVIVGNLDEL IEQHDPFGVV AQYPGTYGHV KDLSELIEKT
HAKKALFCAS ADIMSLIMLK SPGELGADVV FGSAQRFGVP MGYGGPHAAF FATRDAYKRS
VPGRIIGVSV DSRGNQALRM AMQTREQHIR REKATSNICT AQVLLANMAG FYATYHGPQG
LKVIASRIHR MADILATGLQ SKGVELVNNT WFDTITLNLG DKRDSAYDAA LALGINLRKV
GADQLGISCD EKTGRQEILD LWQAIIGADH GLDLEAIDSE LVANGSVSIP AALVRTSAIL
THPVFNTHHS ETEMLRYLKQ LENKDISLTH AMIALGSCTM KLNATAEMIP VSWPEFGSMH
PFAPIDQAAG YSEMINSLEE MLKAITGFDA ICMQPNSGAQ GEYAGLLAIR NFHIANGDDH
RNICLIPSSA HGTNPASAAL ADMKVVIVGC DDQGNVDMDD MRAKAEQHAE NLSCLMITYP
STHGVYEESI REICEIIHEN GGQVYMDGAN MNAQVAISQP GEIGADVSHL NLHKTFCIPH
GGGGPGMGPI GIKAHLAPFV ANHPVQKIDG PKPDNGAVSA APWGSASILP ITWVYIALMG
QPGLRKATEV AILNANYLTK KLGEHYSVLY TGRNDKVAHE CIIDLRPLKD SSGISEEDVA
KRLMDYGFHA PTMSFPVAGT LMIEPTESEP KAEIDRFIEA MIAIRQEIAD VEAGKLNAEQ
NPLKGAPHTM EDLIDPKWDR PYSPVLGAFP LDSVKANKFW PTVNRIDNVY GDRNLFCACP
SMESYAQD
//
