GCSP_SYNY3
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 25-MAY-2022, entry version 125.
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=slr0293;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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=(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; 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; 1148.1653603; -.
DR PaxDb; P74416; -.
DR PRIDE; P74416; -.
DR EnsemblBacteria; BAA18516; BAA18516; BAA18516.
DR KEGG; syn:slr0293; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR InParanoid; P74416; -.
DR OMA; CVPMSEY; -.
DR PhylomeDB; P74416; -.
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; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 1.
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 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
