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Database: UniProt
Entry: M1WYV7_9NOST
LinkDB: M1WYV7_9NOST
Original site: M1WYV7_9NOST 
ID   M1WYV7_9NOST            Unreviewed;       968 AA.
AC   M1WYV7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=RINTHH_780 {ECO:0000313|EMBL:CCH66233.1};
OS   Richelia intracellularis HH01.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX   NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH66233.1, ECO:0000313|Proteomes:UP000053051};
RN   [1] {ECO:0000313|EMBL:CCH66233.1, ECO:0000313|Proteomes:UP000053051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH01 {ECO:0000313|EMBL:CCH66233.1,
RC   ECO:0000313|Proteomes:UP000053051};
RA   Hilton J.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051};
RA   Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA   Villareal T.A.;
RT   "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT   metabolism enzymes.";
RL   Submitted (JAN-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:ARBA00033655, 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}.
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:CCH66233.1}.
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DR   EMBL; CAIY01000005; CCH66233.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1WYV7; -.
DR   STRING; 1165094.RINTHH_780; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000053051; Unassembled WGS sequence.
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:UP000053051}.
FT   DOMAIN          29..454
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          482..745
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          787..908
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         715
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT                   ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   968 AA;  106153 MW;  691D838BEAC8B910 CRC64;
     MASQALYPEC SSSQSTDGNF SAQSLTFKQR HIGPDSHYVK KMLGVLEVKT LDDLIDKVIP
     PNIRLNRFLQ LPTALSEYAA LGNLKNIAAQ NQVFRSFIGM GYYQCIIPAV IQRNILENPG
     WYTAYTPYQP EIAQGRLEAL LNFQTMIIDL TGLEIANASL LDEGTAAAEA MNMSYGATKH
     KTHNFFVSQD CHPQTIDVLQ TRARPLGINI IIGNHITFDF SQPIFGAVLQ YPASDGSIYK
     YHVFIEQAHA EGALVTVAAD PLSLTLLEPP GEFGADIAVG STQRFGSPMG YGGPHAGYFA
     TKEKYKRQVP GRVVGVSKDT HGNIAYRLSL QTREQHIRRE KATSNICTAQ VLLAVIASMY
     AVYHGAAGLK VIALEIHQHT VTLAEGLKQL GYNITNKYFF DTLRVDLGPR SVKDILAACK
     LKKINLRLFS DSSVGISLDE TTTIKDIEDL LGIFAGNSHT PSRKLLPPQL PLEISRTSNY
     LTHPVFNSYH SETELLRYLH KLELKDLSLT TSMIPLGSCT MKLNATSEMM PVTWPEFSNI
     HPFAPQSQTK GYQVIFQQLE NWLAEITGLA GVSLQPNAGS QGEYAGLLVI RKYNESRREG
     HRNICLIPTS AHGTNPASAV MCGMKVVPVA CDNGGNIDID DLKAKAEKHS RELAALMVTY
     PSTHGVFEVA IQEICGVIHD HGGQVYMDGA NMNAQVGLCR PGDIGADVCH LNLHKTFCIP
     HGGGGPGMGP IGVAIHLKPF LPGHSIVEIG DELSMGTVSS APWGSSSILL ISWMYIVMMG
     ADGLTDATKV AILNANYIAK RLESYYPVLY KGTNGLVAHE CILDLRSFKK SAGVEIDDVA
     KRLMDFGFHA PTVSWPVAGT IMVEPTESES LPELERFCEA MITIRKEISE IESGKVDVED
     NLLKNAPHTA TNLLTAKWNH PYSREQAAYP LPWVKNNKFW PAVGRVNAAF GDRNFICSCI
     PMETYSQE
//
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