(data stored in ACNUC7421 zone)

SWISSPROT: E3JB65_FRAIE

ID   E3JB65_FRAIE            Unreviewed;      1020 AA.
AC   E3JB65;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 59.
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   OrderedLocusNames=FraEuI1c_0513 {ECO:0000313|EMBL:ADP78595.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78595.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78595.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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
CC       through its pyridoxal phosphate cofactor; CO(2) is released and
CC       the remaining methylamine moiety is then transferred to the
CC       lipoamide cofactor of the H protein. {ECO:0000256|HAMAP-
CC       Rule:MF_00711}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-lipoyl-L-lysyl-[glycine-cleavage
CC         complex H protein] = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-
CC         lysyl-[glycine-cleavage complex H protein] + CO2;
CC         Xref=Rhea:RHEA:24304, Rhea:RHEA-COMP:10494, Rhea:RHEA-
CC         COMP:10495, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:83099, ChEBI:CHEBI:83143;
CC         EC=1.4.4.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00711,
CC         ECO:0000256|SAAS:SAAS01118902};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00711,
CC         ECO:0000256|PIRSR:PIRSR603437-50,
CC         ECO:0000256|SAAS:SAAS00348850};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H. {ECO:0000256|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|HAMAP-
CC       Rule:MF_00711, ECO:0000256|SAAS:SAAS01082689}.
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DR   EMBL; CP002299; ADP78595.1; -; Genomic_DNA.
DR   RefSeq; WP_013421717.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0513; -.
DR   EnsemblBacteria; ADP78595; ADP78595; FraEuI1c_0513.
DR   KEGG; fri:FraEuI1c_0513; -.
DR   eggNOG; ENOG4105CBI; Bacteria.
DR   eggNOG; COG0403; LUCA.
DR   eggNOG; COG1003; LUCA.
DR   HOGENOM; HOG000239369; -.
DR   KO; K00281; -.
DR   OMA; DEHCHPQ; -.
DR   OrthoDB; 70707at2; -.
DR   BioCyc; FSP298654:G1GOT-510-MONOMER; -.
DR   Proteomes; UP000002484; 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   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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; E3JB65.
DR   SWISS-2DPAGE; E3JB65.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00711,
KW   ECO:0000256|SAAS:SAAS01082684};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW   ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|SAAS:SAAS00426532};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   MOD_RES     741    741       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00711,
FT                                ECO:0000256|PIRSR:PIRSR603437-50}.
SQ   SEQUENCE   1020 AA;  106630 MW;  01095DE58C845D7B CRC64;
     MTENATGTPT LPATSYPVFA DRHIGPDPSA QATMLAELGY PTLAALTDAA VPAGIRSGAL
     ALPTPIPESA ALDELRALAG RNRRVTTMIG LGFHPAVMPG VIQRNVLENP AWYTAYTPYQ
     PEISQGRLEA LLNFQTMVTD LTGLATAGAS LLDESTAAAE AMQLAHRADK AKRSTFLIDA
     DTLPQTIEVV RTRAEALGLD VHVADLRVGL SPIPSPAPGE GPVEALPAEP GEEPQEAAGA
     LPADVLADTF GVLLSYPGAN GEVRDLRGVI AQATGRRIVV TVAADLLALT LLTSPGELGA
     DIAVGTTQRF GLPVMFGGPH AGYLAVRKGL ERNLPGRLVG VSVDADGKPA YRLSLQTREQ
     HIRREKATSN ICTAQVLPAV LASMYAVYHG PAGLAGIAAT VHDHAVRLAA GLRAGGVEVV
     HGSFFDTVLA RVPGRAADVV AAALDHGVNL RLVDGDHVGI SCNEATLDAD LTAVWSAFGV
     AAPDSQAQGA LAVPAELVRT SAYLEHPVFH SHRSETAMLR YLRRLSDVDF ALDRGMIPLG
     SCTMKLNATA EMAAVTWPEF AEIHPFAPVE QAAGYLEMIS DLERWLVEVT GYAGISLQPN
     AGSQGEFAGL LAISSYHRDH TPAGAPARDL CLIPSSAHGT NAASAAMAGM KVVVVACDDD
     GNVDLADLAA KATQHAERLA ALMVTYPSTH GVYEEGIGEA CAIVHAAGGL VYVDGANLNA
     LVGLAKPGEF GADVSHLNLH KTFCIPHGGG GPGVGPVAVG EKLLPYLPNH PLRPEAGPAT
     GVGPISEAPW GSAGILMIPW VYLRLMGAEG VTAATSVAVL NANYVASRLR PHYPVLYAGQ
     NGLVAHECIL DLRQLTKDTG VTVDDVAKRL IDYGFHAPTM SFPVAGTLMV EPTESEDLGE
     IDRFCDAMIA IRAEADKVAD GTWPKDDNPL RNAPHTAEMV TGDAWDHAYP RSVAAYPVTS
     LRAAKYWPPV RRIDGAYGDR NLVCTCPPPE AFATDLTLTD AAPATLPDAR TALTPVGAAG
//

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