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Database: UniProt
Entry: A0A1Y1YXA1_9FUNG
LinkDB: A0A1Y1YXA1_9FUNG
Original site: A0A1Y1YXA1_9FUNG 
ID   A0A1Y1YXA1_9FUNG        Unreviewed;      1015 AA.
AC   A0A1Y1YXA1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE            EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN   ORFNames=K493DRAFT_312043 {ECO:0000313|EMBL:ORY02504.1};
OS   Basidiobolus meristosporus CBS 931.73.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC   Basidiobolus.
OX   NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORY02504.1, ECO:0000313|Proteomes:UP000193498};
RN   [1] {ECO:0000313|EMBL:ORY02504.1, ECO:0000313|Proteomes:UP000193498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY02504.1,
RC   ECO:0000313|Proteomes:UP000193498};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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=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}.
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:ORY02504.1}.
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DR   EMBL; MCFE01000056; ORY02504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1YXA1; -.
DR   STRING; 1314790.A0A1Y1YXA1; -.
DR   InParanoid; A0A1Y1YXA1; -.
DR   OrthoDB; 177349at2759; -.
DR   Proteomes; UP000193498; 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; 2.
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   HAMAP; MF_00711; GcvP; 1.
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:UP000193498};
KW   Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT   DOMAIN          65..492
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          677..793
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          836..957
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         764
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   1015 AA;  111022 MW;  822C5E39BE200F8C CRC64;
     MACSVRVAAR LLTSRTTVTL KSFATPLVVR ALPKPSVAPR FATRFLHTAK PPAKDVFAPL
     DSFPRRHNGS GEKAVDSMLK TIGVKSVDDL IAKTVPSSIR AAKALALDNG YPERELLKRL
     KDIASKNKVY RSYIGMGYTD TVVPNVILRN VMENPAWYTQ YTPYQAEISQ GRLESLLNYQ
     TMVADLTGME IANASLLDEG TAAGEAMVMC YTASRNKKKT FFVDENCHPQ TIEVLKTRAE
     GFGINVVVGN YKTYDFEGAQ KDLSGVLIQY PANDGIVIDY QGFTDRIHQL GGQVVCATDL
     LALTMLKPPG EFGADIVLGN SQRFGVPLGY GGPHAAFFAC TKDNARRMPG RIVGVSKDAA
     GKKALRLALQ TREQHIRREK ATSNICTAQA LLANMAAMYA VYHGPEGIKQ IAQRIHNLTT
     ILSEGIRKAG HTIQNDTFFD TLTINVTGGS ESVIKKAADN GINLRHIDES TVGITLDETV
     TRKDLEDLLK VFSKDGSAPD VSVLASELGV SESKPAQSFP SNLARTSKYL EHQVFHSYHS
     ETEMLRYIHH LQSKDLSLTH SMIPLGSCTM KLNATTEMVP VTWPEFGNIH PFAPADQVEG
     YKIMLDELAQ DLAVVTGFDE VSLQPNSGAQ GEYAGLRTIK AFHESRGEGQ RNVCLIPISA
     HGTNPASAAM AGMKVVIVNC KPNGNLDLDD LKAKAEKHKD QLSAVMVTYP STFGVFEDGI
     KDLCDIIHNN GGQVYMDGAN MNAQIGLCSP GEIGADVCHL NLHKTFCIPH GGGGPGMGPI
     GVKAHLAPFL PGHPLVKTGG EKAIGPISAA PFGSASILPI SWAYIKMMGG KGITEATQQA
     ILNANYMRSR LQDHYKVLYT NENGMCAHEF ILDIRPFGTT AGVEAIDVAK RLQDYGFHSP
     TMSWPVANTL MIEPTESESK AELDRFCDAM ISIREEIREI EEGKQPKQQN ILKNSPHTLD
     RLMADEWKQP YSREQAAYPK GWLRERKFWP SVSRIDDAYG DRNLVCSCPP ISDYQ
//
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