ID A0A2C5YPE5_9HYPO Unreviewed; 1144 AA.
AC A0A2C5YPE5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=CDD80_5879 {ECO:0000313|EMBL:PHH70637.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH70637.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH70637.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH70637.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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:PHH70637.1}.
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DR EMBL; NJES01000603; PHH70637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5YPE5; -.
DR STRING; 2004952.A0A2C5YPE5; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000226431; 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 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:UP000226431};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 106..481
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 576..864
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 899..1020
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1077..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 835
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1144 AA; 125924 MW; FA288371393906DE CRC64;
MALIRASICR FGRAPIISRA VRFYTTSPES AEPTGTNDKL PGPIPYDIPD TSDIKWFRNK
FGGSGPDGKI TDGLFYEQHD SRKTENGARM RNAPLMQRHK KVFGYRHIGP RQEDEAEMLK
ALGPGAETLN SFVKQVIPED VMLPPDKTIV GRQLSEEGVK REFERMQLAN DRKIWMNGGG
YYSVEVPPVI KRNLLENPGW YTSYTPYQAE ISQGRLESLL NFQTMVSDLT GLPVANASLL
DEGTAAAEAM TLSYGNLPSA RAKRGDKVFL VSKEIHKTTK WVMRGRAEGF GIRLMSVDLS
SPEIDQTIKR VGKGLVGVLA QYPDTFGGVQ DFRHLAHLVH EQGALFSVAT DLSALTFLTP
PGEFGADIAV GNSQHFGVPL GFGGPHAAFM AVADSIKRRL PGRLVGVSKD RTGGRALRLA
LQTREQHIRR EKATSNVCTS QALLANMAAM YAIYHGPKQL RTMAIASLRH ARMIQKAAEH
YGLEVCTRTI DPEGRVLSDT VAISDSLDRL GKLQLALAKT HISAGESFTC RELMLAVPAN
FNDTNFTRIV QCFRTMAKRN EMDDAADLAA DIWCKGYEES EERIIEGLPA AVRRTSSFLT
HPVFNSYHSE TELMRYIHHL QSKDLSLIHS MIPLGSCTMK LNAAFQMDLI TSSHVSSSHP
NAPMAFVKGW RQLVLVLNMQ LNSLTGMHST SLQPNSGAQG EFAGLRVIRK YHEENDPEQV
RDICLIPVSA HGTNPASATM AGMKVVTVRC DPRTGNLDLA DLEAKCKLHQ DHLGAIMVTY
PSTYGVFEPD IRKVCDMVHE YGGQVYMDGA NMNAQIGLTS PGALGADVCH LNLHKTFCIP
HGGGGPGVGP ICVKEHLNKF LPHKLGRPRV SSALYGSASI LPISWAYLSA MGDDSLVRAT
KIALLNANYM LARLKEHYLI LYTNDKGRCA HEFIIDARHF KATSGIEAID IAKRLQDYGF
HAPTMSWPVP NTLMIEPTES ESKAELDRFV DAMISIRKEI AEIESGRQPR AGNVLKMAPH
TQADIIDGDG DGSWNRPYSR QQAAYPLPWL REKKFWPSVT RVDDAHGDTN LFCTCPPIED
GTNEANMSDQ VTAKTEPEPE PETTPTKADE LQAAVDKVEA EAMESLPATS EPSKDGADGN
VKKP
//
