ID   GCSP_TRIV2              Reviewed;         974 AA.
AC   Q3M9G1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=Ava_2762;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00711};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00711}.
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DR   EMBL; CP000117; ABA22375.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M9G1; -.
DR   SMR; Q3M9G1; -.
DR   STRING; 240292.Ava_2762; -.
DR   KEGG; ava:Ava_2762; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_3; -.
DR   Proteomes; UP000002533; 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; Pyridoxal phosphate.
FT   CHAIN           1..974
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045565"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         722
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   974 AA;  106624 MW;  2BA5DCABC5F1E5C9 CRC64;
     MVSYASIRQS SDEADSTVDA SQKLDARKQD LNNFIQRHIG PSSADIQHML DVLGFSSLDD
     LIEKTVPSTI RLHKKLQLPT AQTEYAALAK LKQIASKNQV FRSYIGMGYY DTITPPVIGR
     NILENPGWYT AYTPYQPEIA QGRLEALLNF QTMIIDLTGL EIANASLLDE ATAAAEAMSM
     SYGVSKNKAN AYFVSHDCHP QTIDVLQTRA KPLGIEIIIG DHQTFDFQKP IFGAVLQYPA
     SDGTIYDYRA FIETAHAQGA LVTVAADPLS LTLLTPPGEF GADIAVGSTQ RFGIPLGFGG
     PHAAYFATKE EYKRQVPGRI VGVSKDVNGK TALRLALQTR EQHIRREKAT SNICTAQVLL
     AVMASMYAVY HGPEGLKQIA ENIHQLTVTL AEGLKRLGYK ISSEHFFDTL RVELGTNNLE
     TILAGCQARN INLRIFDETA VGISLDETTT PEDLIDLWQI FAGEDNLPFT PEELISSLNL
     PLRSSSYLTH PVFNRYHSET ELLRYLHRLE TKDLSLTTSM IPLGSCTMKL NATSEMIPVT
     WEEFGRIHPF APLTQTRGYQ ILFQQLEAWL AEITGFAGVA LQPNAGSQGE YTGLLVIRQY
     HESRGETHRN VCLIPTSAHG TNPASAVMCG MKVVAVACDA GGNIDIDDLK AKAEKHSHEL
     AALMVTYPST HGVFEAGIQE ICAVIHSHGG QVYMDGANMN AQVGICRPGD IGADVCHLNL
     HKTFCIPHGG GGPGMGPIGV ASHLVRFLPG HPVLGSGKNP QNIGAVAAAP WGSASILVIS
     WMYIAMMGAD GLTQATKVAI LNANYIAKRL ETYYPVLYKG QNGLVAHECI LDLRALKKSA
     NIEIDDIAKR LIDYGFHAPT VSWPVTGTIM VEPTESESQA ELDRFCDALI AIRQEIAAIE
     AGKMDTHNNL LKNAPHTIES LIVGEWLHPY SREQAAYPVS WTREYKFWPS VGRIDAAFGD
     RNFVCSCLPM EAYN
//