ID A4CX96_SYNPV Unreviewed; 978 AA.
AC A4CX96;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=WH7805_10209 {ECO:0000313|EMBL:EAR17896.1};
OS Synechococcus sp. (strain WH7805).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR17896.1, ECO:0000313|Proteomes:UP000001224};
RN [1] {ECO:0000313|EMBL:EAR17896.1, ECO:0000313|Proteomes:UP000001224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224};
RA Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F.,
RA Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., Post A.,
RA Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K.,
RA Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00033655, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAR17896.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAOK01000005; EAR17896.1; -; Genomic_DNA.
DR RefSeq; WP_006042842.1; NZ_CH724168.1.
DR AlphaFoldDB; A4CX96; -.
DR STRING; 59931.WH7805_10209; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_0_3; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 9801272at2; -.
DR PhylomeDB; A4CX96; -.
DR Proteomes; UP000001224; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 22..454
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 493..749
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 793..914
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 721
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 978 AA; 105472 MW; 21059E262787F0A7 CRC64;
MTLLDQRTAA SKTVQPISPF VRRHIGPEPQ AVDQMLQALG FADLDAFIQA VVPGDILDPE
PPCADLPEGV DEAPALAELR TIASCNQLSR SLIGLGYFET VTPALIQRQV LENPSWYTAY
TPYQAEIAQG RLEALLNFQT LISELTGLPI ANASLLDEAT AAAEAMSMSF GVCKREGANR
FLVDAAVLPQ TLAVLRTRCE PIGVQLDVAE PEAFRWGDDV FGVLLQLPGR CGRLWDPRAC
IERAHTHGAL VTVSVDPLAQ VLLEPVGALG ADIAVGSAQR FGVPMGGGGP HAAFFATRDA
YRRQVPGRLV GQSRDAEGRP ALRLALQTRE QHIRRDKATS NICTAQVLLA VMASFYAIHH
GPEGLETIAN RIVMLRSRLE LGLAALGFPV PGGVRFDSVD VHCPQAPLVH RLAAREGYNL
RVLPDGVPAD EAHGFGISLD ELSDEAEIQS LLSICAEVVQ TVPPVSSQPS SPAEVMAGVP
LRQRPWLQQS VFHRYRSETE LMRYIQRLVS KDLSLVHGMI PLGSCTMKLN AAAELAPVSW
REFAAVHPFA PVAQQEGFQA LIRDLERWLA ALTGFAGVSL QPNAGSQGEY AGLLVIRAWH
RSRGEAQRDV CLIPTSAHGT NPASAVMAGL RVVAVACDEE GNVDVGDLRS KAREHADVLA
ALMVTYPSTH GVFETRIREI CSLVHEHGGQ VYLDGANLNA QVGLCRPGAF GADVCHLNLH
KTFCIPHGGG GPGVGPIGVA AHLQPFLPGH PLMPCGGNQP ISSVSAAAWG SAGILPISWM
YLRMMGAEGL RTATAVALLS ANYLAHRLHA HYPVLFRGEG GLVAHECILD LRGLKRSAGL
EVDDLAKRLM DYGFHAPTVS WPVAGTVMVE PTESESLEEL DRFCDAMIAI REEVSRIESG
ESDRDNNPLK RSPHTLAAVT DDHWERPYSR QEAAFPLPGQ QQNKFWPAVA RIDNAFGDRN
LICTCPSVAE LAESLPVR
//