ID A0A0F4GPB9_9PEZI Unreviewed; 1060 AA.
AC A0A0F4GPB9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=TI39_contig365g00005 {ECO:0000313|EMBL:KJX99274.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX99274.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX99274.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX99274.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) 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:KJX99274.1}.
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DR EMBL; LAFY01000357; KJX99274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GPB9; -.
DR STRING; 1047168.A0A0F4GPB9; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000033647; 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:UP000033647};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 78..528
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 548..823
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 867..988
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 794
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1060 AA; 115680 MW; 94D13163BAC71F91 CRC64;
MSATALRLRA QWLATRRPLS PRCLIVKQPA VRCPTLARAK HTTTRGFYSS SSADSESGKP
KTQIDNASLF APLDTFARRH IGPTAESTEE MLKVLDPPAS SLDEFVAQVL PSTILSKKDL
RVEGPIPESG SVPSESGGYS ESQLLTRLRQ IASENKVYKS YIGCGYAGTR VPEVIKRNIL
ENPAWYTSYT PYQPEISQGR LESLLNYQTM VCDLTGLAIS NASVLDEATA AAEAMTLSMN
AMPASRLKRP NKTYFVSHLC HPQTLAVLES RAHGFGIRIE VGDVLANNSS RVEELGEDLI
GVLAQYPDTL GGVEDYRGLA DKVHKLKGTF AVATDLLALT LLTPPGEFGA DVAFGNAQRF
GVPFGFGGPH AAFFAVSEKH KRKIPGRLIG LSKDRLGNTA ARLALQTREQ HIRREKATSN
ICTAQALLAN MSAMYAVYHG PAGLKKIAEK VAKMAQVLAK GLESGGLEVR QPVAFDTVVV
KKHDARGFVT KTAQNFMTNF RVIDDEHVGI TVDETVGKKQ IEEIFRAFTT DDVDIDQLAQ
SVTATGGVPK SLVRTSEYLT HPVFNSYHSE TEILRYMYHL QSKDLSLVHS MIPLGSCTMK
LNATTEMVPI SWPEFANIHP FAPSDQTKGY AKMIGELEAD LSEITGFHSV SLQPNSGAQG
EFAGLRVIRK YQEDQPGKKR DICLIPVSAH GTNPASAAMA GMRVVTIKCD PDTGNLDMVD
LKAKCEKYSE ELGAIMITYP STFGVFEPQV KEACDIVHKH GGQVYMDGAN MNAQIGLCSP
GEIGADVCHL NLHKTFCIPH GGGGPGVGPI GVAKHLSPYL PGHPLVANVG GEKAIAPISG
APWGSASILP ISWAYIKMMG ARGLTHATKI TLLNANYIQS RLKSHYPILY TNDNGRCAHE
FILDTRKFKE TAGIEVIDIA KRLQDYGFHS PTMSWPVANT LMIEPTESES KNELDRFCDA
LISIREEIAE IEQGKQPRDG NVLKMAPHSM KDLILSKWDR PYTRENAAYP LDYLKEKKFW
PTVTRLDDAY GDMNLFCSCA PVESLEQVEG LTGAAAPMPT
//
