ID   GCSP_NOSS1              Reviewed;         983 AA.
AC   Q8YNF9;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=all4607;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB76306.1; -; Genomic_DNA.
DR   PIR; AG2381; AG2381.
DR   AlphaFoldDB; Q8YNF9; -.
DR   SMR; Q8YNF9; -.
DR   STRING; 103690.gene:10496657; -.
DR   KEGG; ana:all4607; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002483; 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; Reference proteome.
FT   CHAIN           1..983
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166902"
FT   MOD_RES         731
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   983 AA;  107753 MW;  3255D178ED6CC6F0 CRC64;
     MVSYASIPQS SDEAHSTVGA SLQLDERKQD LNNFIQRHIG PSSADIQQML DVLGFSSLDD
     LIEKTVPSAI RLHEQLQLPE AQTEYAALAK LKQIASKNQV FRSYIGMGYY DTITPSVIGR
     NILENPGWYT AYTPYQPEIA QGRLEALLNF QTMIIDLTGL EIANASLLDE ATAAAEAMSM
     SYGVSKNKAN AYFVSHDCHP QIIDVLQTRA KPLGIEIIIG DHQTFDFDKP IFGAVLQYPA
     SDGTIYDYRA FIETSHAQGA LVTVAADPLS LTLLTPPGEF GADIAVGSTQ RFGIPLGFGG
     PHAAYFATKE EYKRQVPGRI VGVSKDVHGK TALRLALQTR EQHIRREKAT SNICTAQVLL
     AVMASMYAVY HGPEGLKQIA ERIHHLTLVL GVWLQRLGYT ITSQSFFDTL QIKLGEKPLQ
     EILEAAEAYR INLRIVDTST VGISLDETTT LEDVKDICRI FAGTDELPFV LNVQEFDWII
     QQSSLKDEPF SRQSSYLTHP VFNRYHSETE LLRYLHRLET KDLSLTTSMI PLGSCTMKLN
     ATSEMIPVTW EEFGRIHPFA PLTQTRGYQI LFQQLEAWLG EITGFAGVSL QPNAGSQGEY
     TGLLVIRQYH QSRGETHRNV CLIPNSAHGT NPASAVMCGM KVVAVACDAG GNIDIDDLKA
     KAEKHSHELA ALMVTYPSTH GVFEAGIQEI CAVIHSHGGQ VYMDGANMNA QVGICRPGDI
     GADVCHLNLH KTFCIPHGGG GPGMGPIGVA SHLVPFLPGH PVLESGKNPQ NIGAVAAAPW
     GSASILVISW MYIVMMGADG LTQATKVAIL NANYIAKKLA AYYPVLYKGQ NGLVAHECIL
     DLRALKKSAN IEIDDIAKRL IDYGFHAPTV SWPVAGTIMV EPTESESQAE LDRFCEALIA
     IRQEIADIEA GKVDIQDNSL KNAPHTVESL IVGEWPHPYS REQAAYPAPW TREHKFWPSV
     GRIDAAFGDR NFVCSCLPMD AYN
//