GCSP_NOSS1
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 25-MAY-2022, 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}; OrderedLocusNames=all4607;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; 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=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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; 103690.17133744; -.
DR EnsemblBacteria; BAB76306; BAB76306; BAB76306.
DR KEGG; ana:all4607; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OMA; CVPMSEY; -.
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; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR003437; GcvP.
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 PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
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