(data stored in SCRATCH zone)

SWISSPROT: C1ASV2_RHOOB

ID   C1ASV2_RHOOB            Unreviewed;       950 AA.
AC   C1ASV2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 68.
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   ECO:0000313|EMBL:BAH48884.1};
GN   OrderedLocusNames=ROP_06370 {ECO:0000313|EMBL:BAH48884.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48884.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48884.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48884.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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: Glycine + [glycine-cleavage complex H
CC       protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H
CC       protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|SAAS:SAAS00731757}.
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:SAAS00731796};
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:SAAS00731791}.
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DR   EMBL; AP011115; BAH48884.1; -; Genomic_DNA.
DR   RefSeq; WP_012687889.1; NC_012522.1.
DR   STRING; 632772.ROP_06370; -.
DR   EnsemblBacteria; BAH48884; BAH48884; ROP_06370.
DR   KEGG; rop:ROP_06370; -.
DR   PATRIC; fig|632772.20.peg.697; -.
DR   eggNOG; ENOG4105CBI; Bacteria.
DR   eggNOG; COG0403; LUCA.
DR   eggNOG; COG1003; LUCA.
DR   HOGENOM; HOG000239369; -.
DR   KO; K00281; -.
DR   OMA; QTMVCDL; -.
DR   OrthoDB; POG091H03O6; -.
DR   Proteomes; UP000002212; 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-HAMAP.
DR   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 3.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASV2.
DR   SWISS-2DPAGE; C1ASV2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00711,
KW   ECO:0000256|SAAS:SAAS00731778, ECO:0000313|EMBL:BAH48884.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW   ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|SAAS:SAAS00731731}.
FT   MOD_RES     701    701       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00711,
FT                                ECO:0000256|PIRSR:PIRSR603437-50}.
SQ   SEQUENCE   950 AA;  100280 MW;  E65A977EACA7F4C8 CRC64;
     MIDAGSRTFA DRHVGPNAAE LAHILELVGA DSLDDLASKA VPAVILDGVT GGIADGLDAL
     PAPVSEHEAL AELSALAAQN TVATSMIGLG YYDTLTPPVL IRNIIENPAW YTAYTPYQPE
     ISQGRLEALL NFQTMVADLT GMEVANSSML DEATAAAEAM TLLRRASKSK SPRFVVDADL
     FPQTLAVVET RAEPLGIEIV VADLSAGLPD GDFFGVLGQM PGASGRIADY TDVIAAAHER
     GALVAVGADL LALTLLTPPG EIGADACFGT TQRFGVPMGF GGPHAGYLAV HTKHARQLPG
     RLVGVSVDAD GDKAYRLALQ TREQHIRREK ATSNICTAQV LLAILAAMYA SYHGAEGLKA
     IALRVAATAH SLAAALRGTG ATVVHEHFFD TILVRVDGRA ADVVAKAKDA GINLRLVDAD
     HVAVACDEAT TDDDVARVLA AFGGDGPVAR EAGTSVPESQ LRGSDYLQHE AFTRYRTETA
     MLRYLRALSD KDIALDRSMI PLGSCTMKLN ATAEMEAITW PAFAGLHPFA PTGDTPGILR
     IIKDLENWLV AVTGYDAVSL QPNAGSQGEY AGLLAIRNYH LSRGDDHRDT CLIPSSAHGT
     NAASAVMAGM RVEVVACRPN GDVDLDDLRA KIADHAERLA AIMITYPSTH GVYEHEIADI
     CAAVHDAGGQ VYVDGANLNA LVGLARPGRF GGDVSHLNLH KTFCIPHGGG GPGVGPIGVR
     SHLTPFLPGH PLAPELGTAG PISAAPYGSA SILPITWAYI RMMGAVGLRR ASLTAIASAN
     YIARRLDEYF PVLYTGEGGM VAHECILDLR PITKDTGVTV DDVAKRLADY GFHAPTMSFP
     VAGTLMVEPT ESENLEEIDA FCEAMIAIRA EIDRVGSGEW TVDDNPLRGA PHTAGCLAAE
     WNHPYTRETA VFPRGKARPK VWPAVRRIDG AHGDRNLVCS CPPISAFEGA
//

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