(data stored in SCRATCH zone)

SWISSPROT: Q6BMN9_DEBHA

ID   Q6BMN9_DEBHA            Unreviewed;      1035 AA.
AC   Q6BMN9;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE            EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN   OrderedLocusNames=DEHA2F03806g {ECO:0000313|EMBL:CAG88846.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88846.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88846.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000256|RuleBase:RU364056}.
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|RuleBase:RU364056};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR603437-50,
CC         ECO:0000256|RuleBase:RU364056};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H. {ECO:0000256|RuleBase:RU364056}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion
CC       {ECO:0000256|RuleBase:RU364056}.
CC   -!- SIMILARITY: Belongs to the GcvP family.
CC       {ECO:0000256|RuleBase:RU364056}.
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DR   EMBL; CR382138; CAG88846.2; -; Genomic_DNA.
DR   RefSeq; XP_460532.2; XM_460532.1.
DR   STRING; 4959.XP_460532.2; -.
DR   EnsemblFungi; CAG88846; CAG88846; DEHA2F03806g.
DR   GeneID; 2903437; -.
DR   KEGG; dha:DEHA2F03806g; -.
DR   HOGENOM; HOG000239369; -.
DR   InParanoid; Q6BMN9; -.
DR   KO; K00281; -.
DR   OMA; QTMVCDL; -.
DR   OrthoDB; 390348at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 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; Q6BMN9.
DR   SWISS-2DPAGE; Q6BMN9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Mitochondrion {ECO:0000256|RuleBase:RU364056};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364056};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50,
KW   ECO:0000256|RuleBase:RU364056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT   MOD_RES     771    771       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR603437-50}.
SQ   SEQUENCE   1035 AA;  113489 MW;  A2C6463BDC4AE8E4 CRC64;
     MISRVVARSA RANRLSTLTR SVPRAYNLNL KLAASNRFLA SKADTSSADY EKVYDPSAKT
     VSLGNLDTFA RRHLGPTPEN VKTMLSALGY KDLDEFLSKA IPEHVLYKRA LQIQPQQGFT
     ESEMLEHLHN LANKNKIVKS FIGKGYAGTK VPPVIQRNLL ESPEWYTSYT PYQPEISQGR
     LESLLNYQTM VTSLTGLNMA NASLLDEGTA AGEAMSLSFH SLKGKRGKYA VDTNLHPQTL
     DVMKSRAENI GVEIVELPLS TQEGLEELER IASDSCGALV QYPGTDGSLN NYTKVGEIVH
     AHKGLFAMAT DLLALTLIKS PAEFNADIAL GTSQRFGVPF GYGGPHAAFF ATNMKYSRKI
     PGRIVGLSKD RLGKPALRLA LQTREQHIKR EKATSNICTA QALLANMAAM YAVYHGPKGL
     KDIASRVYGY TTVLANEISN NSQHEIVNDK WFDTLTVKLG GGVKSDEILN KALNEYNINL
     FKAGEDKVSL CLDETVEEKD LIALVDVFTG NDSFSTSSIS ELPKLPTELL RTDEILAHPV
     FNTHRSETSM LRYLHLLQSR DLSLANSMIP LGSCTMKLNA TVEMQTLSMP GFNQIHPFAP
     LNQAQGYKEL VDEFEKDLND ITGFDATTNM PNSGAQGEYT GLSLIRQYHK SKGEYEQRNI
     CLIPVSAHGT NPASAAMCGL KVVPVKCLNN GSIDVDDLKV KAEKHAENLC SIMITYPSTY
     GLFEPGIKTA IDLVHNNGGL VYLDGANMNA QVGLTSPGDL GADVCHLNIH KTFALSHGGG
     GPGQAPVCVK EHLKPFLPKH HFLDTPHSTN ESIQAVNSAP YGSASVIPVS YSYIKMLGAK
     ALPHVSSIAM LNANYMLEKL KDDYQIMFVD HSASTDEGLK HCAHEFILDL REFKAVGVEA
     IDVAKRLQDY GFHAPTMSFP VAGTLMIEPT ESENLEELDR FINSLLSIRK EINAMANKEP
     LGQVLKNAPH SLNDIVSTSQ ADWEARGYTR EQAAYPLPFL KESKCWPSVS RVDDTYGDMN
     LMCTCPSVEE VAADQ
//

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