ID G0RTL4_HYPJQ Unreviewed; 976 AA.
AC G0RTL4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=TRIREDRAFT_81339 {ECO:0000313|EMBL:EGR45383.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR45383.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR45383.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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)-[(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:ARBA00043839,
CC ECO:0000256|RuleBase:RU364056};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|RuleBase:RU364056};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|RuleBase:RU364056}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|RuleBase:RU364056}.
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DR EMBL; GL985079; EGR45383.1; -; Genomic_DNA.
DR RefSeq; XP_006968584.1; XM_006968522.1.
DR AlphaFoldDB; G0RTL4; -.
DR STRING; 431241.G0RTL4; -.
DR EnsemblFungi; EGR45383; EGR45383; TRIREDRAFT_81339.
DR GeneID; 18489313; -.
DR KEGG; tre:TRIREDRAFT_81339; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_81339; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
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; 1.
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 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 Mitochondrion {ECO:0000256|RuleBase:RU364056};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364056};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50,
KW ECO:0000256|RuleBase:RU364056};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 18..393
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 471..753
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 790..911
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 726
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 976 AA; 107099 MW; 5E73A5552C684CE3 CRC64;
MRQIRAANKL PWKDFSARHI GPRDDEIEQM LKALGPGAET LDAFVSQVIP ADVLDPPKKT
IQSHVYSESG IVKAFKNMNA HNDIRVWMNG GGYYPVEIPA VIKRNVLENP AWYTSYTPYQ
PEISQGRLES LLNFQTMVSD LTGLPVANAS LLDEGTAASE AMTMSLTSLP ASRQKRSGKT
YVVSHLVHDA TIRVMHGRAE GFGIHIQVLD LGAPDAQDKI KALGDDLIGV MVQYPDSNGG
VSDFRELAEL AHAQGTLLSA ATDLSNLTLL TPPGEWGADI AFGNAQRFGV PLGYGGPHAA
FMAVQEGSKR RLPGRLIGVS RDRRGDRALR LALQTREQHI RREKATSNVC TAQALLANMS
AMYAIYHGPE QLREMAINNL RHARMIQAAA QHYGLNVSTR SVDADGKVLS DTVALHFDDP
VVCRALRREL MDQGISSGKA WQPNELTVAY KNHSDADLDV SAKYWKEGFA QSSEELIQSL
PESVRRQSKF LTHPVFNSHH SETEMLRYMY HLQSKDLSLV HSMIPLGSCT MKLNGTTQME
LIGLENASNI HPHAPYSCAK GYQRLFDATS AQLAALTGMD GTSLQPNSGA QGEFAGLRAI
RKYHEQQPGP KRDICLIPVS AHGTNPASAA MVGMRVVPIK CDTKTGNLDL EDLEAKCKKH
ASELGAIMIT YPSTYGVFEP QVRKVCDIVH QYGGLVYMDG ANMNAQIGLT SPGALGADVC
HLNLHKTFCI PHGGGGPGIG PICVKKHLIP YLPHKSTQTP VSSAAFGSAS IVPISWSYIS
TMGDAGLRKA TTVALLNANY LLTRLKDHYP ILYTNDKGRC AHEFIVDARP FQKTAGIEAI
DIAKRLQDYG FHAPTMSWPV PNTLMIEPTE SESKEELDRF VDAMISIRNE IREIEEGKQP
RQGNVLKNAP HPQRDLILGD AEGKWDRPYS REKAAYPLPY LLEKKFWPTV GRVDDTYGDT
NLFCTCPPVE DTTGSA
//
