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Database: UniProt
Entry: A4CX96_SYNPV
LinkDB: A4CX96_SYNPV
Original site: A4CX96_SYNPV 
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}.
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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
//
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