ID   GCSP_SYNY3              Reviewed;         983 AA.
AC   P74416;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=slr0293;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18516.1; -; Genomic_DNA.
DR   PIR; S76257; S76257.
DR   PDB; 4LGL; X-ray; 2.00 A; A/B=1-983.
DR   PDB; 4LHC; X-ray; 1.90 A; A/B=1-983.
DR   PDB; 4LHD; X-ray; 1.80 A; A/B=1-983.
DR   PDBsum; 4LGL; -.
DR   PDBsum; 4LHC; -.
DR   PDBsum; 4LHD; -.
DR   AlphaFoldDB; P74416; -.
DR   SMR; P74416; -.
DR   IntAct; P74416; 2.
DR   STRING; 1148.gene:10499397; -.
DR   PaxDb; 1148-1653603; -.
DR   EnsemblBacteria; BAA18516; BAA18516; BAA18516.
DR   KEGG; syn:slr0293; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   InParanoid; P74416; -.
DR   PhylomeDB; P74416; -.
DR   BioCyc; MetaCyc:MONOMER-22025; -.
DR   BRENDA; 1.4.4.2; 382.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..983
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166942"
FT   MOD_RES         726
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
FT   HELIX           16..26
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           33..37
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           42..52
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           57..64
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           83..94
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           115..120
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           125..128
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           140..157
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           169..182
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           199..209
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          215..219
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           221..223
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          230..238
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           248..256
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          260..265
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           276..279
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          282..287
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            289..292
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           309..314
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          319..325
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          330..335
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           337..339
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           341..344
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           357..395
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          403..412
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           418..427
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          439..443
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           450..461
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          463..465
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           471..476
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           483..485
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           495..497
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           503..515
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            520..522
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            528..530
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           537..540
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           541..544
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           546..549
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           557..559
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           561..578
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          581..584
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           590..607
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          615..619
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           625..632
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          636..640
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          646..648
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           650..659
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           661..663
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          664..672
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           682..691
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          695..700
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           703..705
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            706..709
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           712..714
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          718..722
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            724..728
FT                   /evidence="ECO:0007829|PDB:4LGL"
FT   TURN            733..735
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          742..744
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           746..749
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          773..776
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           781..783
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           784..817
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   TURN            818..820
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          823..825
FT                   /evidence="ECO:0007829|PDB:4LGL"
FT   HELIX           828..830
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          836..839
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           841..847
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           851..860
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          867..869
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          875..878
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           886..907
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          913..916
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           917..920
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           925..929
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          935..937
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           939..943
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           947..950
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   HELIX           963..968
FT                   /evidence="ECO:0007829|PDB:4LHD"
FT   STRAND          970..972
FT                   /evidence="ECO:0007829|PDB:4LGL"
FT   HELIX           974..976
FT                   /evidence="ECO:0007829|PDB:4LHC"
SQ   SEQUENCE   983 AA;  107322 MW;  4009367B62A2936F CRC64;
     MPNLEPAVVV PTSEAIAVDL TKLEEKLAPA DSFLDRHLGP GETEQRQMLQ TLGFDTLGDL
     IDQAVPPAIR FPRSLQLPAS QSEYGAIAQL KSIASKNQVF RSYIGMGYYD TITPPVIQRN
     ILENPGWYTA YTPYQAEIAQ GRLEALLNFQ TMVMDLTGLE IANASLLDEG TAAAEAMALS
     YGVSKSKANA FFVAQDCHPQ TIEVIKTRAN PLGIEVIVGD HHTFSFSTSI FGALLQYPAT
     DGAVYDYRSF IDKAHQHQAL VTLAADPLSL TLLTPPGELG ADIAVGSTQR FGIPLGYGGP
     HAAYFATKAE YQRKMPGRIV GVSKDAHGNP ALRLALQTRE QHIRRDKATS NICTAQVLLA
     VMASMYGVYH GSTGLKNIAL RIHQLTVLLA IGLKRLNYSL NNDYFFDTLR VGVGEQSAPA
     ILKAAEGRGI NLRPLVPGEV GISLDETVTV QDLLDLWQVF AGKDNLPFTP EELWSEVKTS
     FPADLTRQSL YLQDAVFNQY HSETELLRYL HQLESKDLAL NTSMIPLGSC TMKLNATAEM
     MPVTWPEFGK IHPFAPAGQT EGYQILFAQL EAWLGEITGF DAISLQPNAG SQGEYAGLQV
     IRQYHLSRGE EQRNICLIPE SAHGTNPASA VMCGMQVVPV KCDGEGNIDV EDLTSKAEKY
     GDRLAALMVT YPSTHGVFEA TIGTICDIVH RFGGEVYMDG ANMNAQVGLC RPADFGADVC
     HLNLHKTFCI PHGGGGPGMG PIGVKSHLQA FLPRTSLNST AELQAEDQSI GMISAAPYGS
     ASILVISWMY IAMMGPQGLT KATEVAILSA NYMAKRLENY YPILFRGNNE LVAHECILDL
     RPLKKQAAIE VEDVAKRLMD FGFHAPTVSW PVLGTMMVEP TESESLGELD RFCDAMIAIY
     QEAQAITHGE IDPADNPLKN APHTAQSLIC GEWNHPYSQE EAAYPAPWTK QFKFWPAVGR
     INNTYGDRHL VCSCEGMEAY KEG
//