ID A0A3D8QJV9_9HELO Unreviewed; 1062 AA.
AC A0A3D8QJV9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=BP6252_11528 {ECO:0000313|EMBL:RDW62095.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW62095.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW62095.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW62095.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW62095.1}.
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DR EMBL; PDLM01000014; RDW62095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8QJV9; -.
DR STRING; 1849047.A0A3D8QJV9; -.
DR Proteomes; UP000256645; 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:UP000256645};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 83..536
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 583..838
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 881..1002
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 809
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1062 AA; 115520 MW; 9C12DF146372CBCC CRC64;
MAVSSLAVRA QVGRAAITAR AAATRSSQLS RSWAYRPFIR APGSFPIPLR RSFYTSSSSD
ESNTVPSAKL SNGSYPPLDT FARRHIGPSA DSTEQMLKAL DPPASSLDEF VKQVLPSDIL
SSKNLGIDAS TSEGDAGFTE SQLLARLRSI ASKNTIMRSY IGCGYAGTRV PEVIKRNVLE
GPGWYTSYTP YQPEISQGRL ESLLNFQTLV CDLTALPISN ASLLDESTAA AEAMTLSMNM
LPASRQKSKN KTFFVSHLVH PQTKAVLQSR ADGFGIKIEI GDVMEDEGKR IKELGNDLIG
VLVQYPDTEG GVEDFKALAD IIHSQGATFS VATDLLALTV LTPPGEFGAD IAFGNAQRFG
VPFGYGGPHA AFFAVSDKYK RKIPGRLIGV SKDRLGNPAM RLALQTREQH IRREKATSNV
CTAQALLANM SAFYAVYHGP KGLRNIAERA IHGARIVEQG LNDMGFKTGS RGKGEDGRVL
FDTVVVNVGE GKSDKILTHA IRDYGINLRK FDNNRLGITI DETVDAKDLY EILSIFKEFS
GSSSEIEIES LISSLPGNGT LPIPASLKRS SEYLTHPVFN SHHSETELLR YIHHLQSKDL
SLTHSMIPLG SCTMKLNATT EMAPITWPEF ASIHPFVPTD QAVGYKTMID ELEADLATIT
GFDAVSLQPN SGAQGEFTGL RVIRKFQEQQ PGKKRDICLI PVSAHGTNPA SAAMAGMRVV
TVKCDSKTGN LDMADLKAKC EKYTEELGAI MITYPSTYGV YEPEIKAVCD TVHQHGGQVY
MDGANMNAQI GLCSPGEIGA DVCHLNLHKT FCIPHGGGGP GVGPIGVKSH LAPFLPGHPL
VQTGGEMGIA PVSGAPWGSA SILPISWSYI KMMGGRGLTH ATKVTLLNAN YIMSRLRPYY
PIAYTNANGR CAHEFILDIR GFKETAGIEA IDVAKRLQDY GFHAPTMSWP ISNTLMIEPT
ESESKEELDR FIDALISIRS EIKAVEDGKI PREGNVLKMA PHSQRDLLIG DWERPYSREQ
AAYPLPYLKE KKFWPSVTRL DDAYGDMNLF CTCGPVESVD EA
//
