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Database: UniProt
Entry: A0A2T1EGV5_9CHRO
LinkDB: A0A2T1EGV5_9CHRO
Original site: A0A2T1EGV5_9CHRO 
ID   A0A2T1EGV5_9CHRO        Unreviewed;       964 AA.
AC   A0A2T1EGV5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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:PSB31969.1};
GN   ORFNames=C7B70_11505 {ECO:0000313|EMBL:PSB31969.1};
OS   Chlorogloea sp. CCALA 695.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Entophysalidaceae; Chlorogloea.
OX   NCBI_TaxID=2107693 {ECO:0000313|EMBL:PSB31969.1, ECO:0000313|Proteomes:UP000238278};
RN   [1] {ECO:0000313|EMBL:PSB31969.1, ECO:0000313|Proteomes:UP000238278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 695 {ECO:0000313|EMBL:PSB31969.1,
RC   ECO:0000313|Proteomes:UP000238278};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB31969.1, ECO:0000313|Proteomes:UP000238278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 695 {ECO:0000313|EMBL:PSB31969.1,
RC   ECO:0000313|Proteomes:UP000238278};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-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}.
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:PSB31969.1}.
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DR   EMBL; PVWN01000018; PSB31969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T1EGV5; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000238278; 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:UP000238278}.
FT   DOMAIN          24..450
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          490..746
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          786..907
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   964 AA;  105302 MW;  34F5AE2FC65BE529 CRC64;
     MVVSLPTQAI NDKEILARSP DFLQRHLGSN AAQIQQMLEV LGLASLDDLI DKTVPQSIRY
     NKRLNLPAAL SEQAALTKLK AISLKNDVFR SFIGMGYHNC ITPPVIQRNI LENPGWYTAY
     TPYQPEIAQG RLEALLNFQT VIIDLTGLEI ANASLLDEAT AAAEAMTMSY GISKNKSKAF
     FVSNSCHPQT IEVIQTRAQP LGIEVIVGNH QDFTFEQQVF GGLLQYPATD GTIYDYRAFV
     EKAHTQGALV TVAADILSLT LLMPPGEFGA DIAVGSTQRF GIPLGYGGPH AAYFATKEEY
     KRQVPGRIVG VSKDVKGKTA LRLALQTREQ HIRRDKATSN ICTAQVLLAV MAGMYAVYHG
     AEGLRNIAQD IHDLTAVLAT GLQKLGYKLG STEIFDTVRV ELGDRLIVKG ILKAAQERKI
     NLRDLSNTSL GISLDETTTL VDVQELLEIF ALNSELPFNI EELASQVKVN PPTLKRTSSY
     LTHPVFNSYK SETELLRYLY RLQSKDLSLT TSMIPLGSCT MKLNATAEMM PVTWAEFGNI
     HPFAPLSQTR GYQELFAQLE DWLGEITGFA GISLQPNAGS QGEYTGLLVI RQYHEQRNEG
     HRNVCLIPTS AHGTNPASAV MCGMKVVPVA CDEQGNVDLA DLQAKAQKHS NELAALMVTY
     PSTHGVFEEE IKDICAIVHS HGGQVYMDGA NMNAQVGLCR PGDFGADVCH LNLHKTFCIP
     HGGGGPGMGP IGVMAHLVPF LPGHAVVSLG GQGIGAVAAA PWGSASILTI SWMYIAMMGA
     EGLTQATKVA ILNANYIAHQ LQDHYPVLYK GKAGLVAHEC ILDLRSLKKS ASIEVDDIAK
     RLMDYGFHAP TVSWPVAGTI MVEPTESESK AELDRFCQAM TLIRQEIAEI EQGNADMQDN
     VLKNAPHTAE VLMADAWEHS YSRNSAAYPA SWTREYKFWT AVSRIDNAFG DRNFICSCLP
     MSDY
//
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