ID A0A9P8TU83_9HYPO Unreviewed; 1066 AA.
AC A0A9P8TU83;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=Trco_006946 {ECO:0000313|EMBL:KAH6605239.1};
OS Trichoderma cornu-damae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=654480 {ECO:0000313|EMBL:KAH6605239.1, ECO:0000313|Proteomes:UP000827724};
RN [1] {ECO:0000313|EMBL:KAH6605239.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KA19-0412C {ECO:0000313|EMBL:KAH6605239.1};
RA Kim C.S.;
RT "Chromosome-Level Trichoderma cornu-damae using Hi-C Data.";
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|RuleBase:RU364056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026,
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}.
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:KAH6605239.1}.
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DR EMBL; JAIWOZ010000005; KAH6605239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P8TU83; -.
DR OrthoDB; 6537869at2759; -.
DR Proteomes; UP000827724; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:TreeGrafter.
DR CDD; cd00613; GDC-P; 1.
DR FunFam; 3.40.640.10:FF:000005; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 1.
DR FunFam; 3.90.1150.10:FF:000007; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000827724};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 87..461
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 564..843
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 880..1001
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 816
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1066 AA; 116485 MW; 49B1D141C824653F CRC64;
MAARLAALAR GASLRPSLAL ARHEARLCAR GITYTAKAAA GVRGAGRDDG AGLRRASFEA
LQDDPTYKEM RRIRAENKLP WKDFSARHIG PRDDEIREML RALGPGAETM DAFVSQVVPA
DVLDPPKKAI QPLVYSESGI VRAFKAMNAH NDLRVWMNGG GYYPVEIPAV IKRNVLENPA
WYTSYTPYQP EISQGRLESL LNFQTMVSDL TGLPVANASL LDEGTAAGEA MTMSLTSLPA
SRQKRPGKTY VVSHLVHDST IRVMHGRAEG FGIHIDVLDL SAPDARKKIS ALGDDLIGVM
VQYPDSNGGV SDFRDLADLA HGQGVLLSAA TDLSNLTLLT PPGEWGADVA FGNAQRFGVP
LGYGGPHAAF MAVQEASKRR LPGRLIGVSR DRRGDRALRL ALQTREQHIR REKATSNVCT
AQALLANMSA MYAIYHGPEQ LREMAVNNLR HARMIQAAAR HYGLNVSTAS VDPAGAVLSD
TVALYFDEPV VCRALRRELM DQGISSGKAW SPNELVLAVP TTFTLKLFVR IVKAFQTVAY
KNHSDADLDV SSRCWKEGFA QSSEELVGSL PEPVRRESKF LTHPVFNSHH SETEMLRYMH
HLQSKDLSLV HSMIPLGSCT MKLNGTTQME LIGAESSANI HPHAPYSCAK GYQRLFDATS
AQLAALTGMD ATSLQPNSGA QGEFAGLRAI RKYHEQQPGN KRDICLIPVS AHGTNPASAA
MVGMRVVPIK CDTKTGNLDL EDLEAKCKKH ATELGAIMIT YPSTYGVFEP QVRRVCDIVH
QYGGLVYMDG ANMNAQIGLT SPGALGADVC HLNLHKTFCI PHGGGGPGIG PICVKKHLIP
YLPHKSTQTP VSSAAFGSAS IVPISWAYIS TMGDEGLRKA TTVALLNANY MLARLKDHYP
ILYTNDQGRC AHEFIIDARS FQKTAGIEAI DIAKRLQDYG FHAPTMSWPV PNTLMIEPTE
SESKEELDRF IDAMISIRNE IREIEEGKQP KEGNVLKNAP HPQRDLILGD AEGKWDRPYS
REKAAYPLPY LLEKKFWPTV GRVDDTYGDT NLFCTCPPVE DTTGSA
//
