ID W9YBT8_9EURO Unreviewed; 1069 AA.
AC W9YBT8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=A1O1_03421 {ECO:0000313|EMBL:EXJ90322.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ90322.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ90322.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ90322.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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:EXJ90322.1}.
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DR EMBL; AMWN01000003; EXJ90322.1; -; Genomic_DNA.
DR RefSeq; XP_007722516.1; XM_007724326.1.
DR AlphaFoldDB; W9YBT8; -.
DR STRING; 1182541.W9YBT8; -.
DR GeneID; 19158315; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000019484; 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 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:UP000019484};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 67..527
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 549..822
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 878..998
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 799
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1069 AA; 117575 MW; 3BC841017A2EB5E6 CRC64;
MATPVAAYSR ARLPVTRLLR WTPQRIDPSR LCRRCLSVQQ KRQQNAQPAS HQGPPPAFLE
RDELFSQRHI GPSPHDEVLM VKALDPPAKD LDDFIRQTLP PDILAGSELH LQNAFNKDNT
QGVHEVGIER EMLTLARENK NYTSLIGMGY YGTNTPTVIQ RNVLESPAWY TSYTPYQAEI
SQGRLESLLN FQTLVTDLTG LTIANASVLD EGTAAAEAMT LSMNALPTSR QKKPGKAYVV
SDLCHPQTIA VMESRASGFG INVIVGDILA DDFKLVKEQG DNLIGVLAQY PDTLGGVHNF
QKLSDLVHAA DGTFSVATDL LALTLLKAPG EFGVDVAFGN AQRFGVPLGY GGPHAAFFAC
SEKHKRKIPG RLVGISKDRL GKPALRLALQ TREQHIRREK ATSNICTAQA LLANMSAFYA
IYHGPHGLKK IANRIWAMAK FAQAVLKRKG LKVINQGVRE DGAVLFDTVV VEPASVQQYK
QILRVASEEH VLLRTNVPGS TPEAPRLAFS IDETVSSTTL RKLLQCFGVK YDEYIGGFSD
PDIISKVNDD SLPEGLRRQT SFLTHPVFNQ HHSETELLRY IHHLQSKDLS LVHSMIPLGS
CTMKLNGTTE MMAISYPGFS KIHPFAPIHL TTGYQKLIKR LSRALAAITG MQEVSLQPNS
GAQGEFAGLR VIKKYLDHQD SSKKRNICLI PVSAHGTNPA SAAMAGMKVV PLKCDTKSGN
LDLKDLEEKC KKHKDELAAI MITYPSTFGV FEPGIKEVCK IVHEHGGQVY MDGANLNAQI
GLCNPGEIGA DVCHLNLHKT FCIPHGGGGP GVGPIAVKEH LRPFLPMHPH VDPHPGGETR
ATTAISPVSS APWGSASILP ISYAYIQLMG SAGLKHGTEI ALLNANYIMS RLRPYYPIMY
TNANGRCAHE FILDTRKFKE TAGVEAIDIA KRLQDYGFHA PTMSWPVANT LMIEPTESES
KEELDRFCDA LIEIRKEIQA VEDGNAPREG NVLKMSPHPA IDLMRSAWDR PYSREQAAYP
LPWLREKKFW PSVARVDDAY GDTNLFCTCT PVEGYEEEGI TGHQAPMST
//
