ID R9AGP2_WALI9 Unreviewed; 1031 AA.
AC R9AGP2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=J056_004185 {ECO:0000313|EMBL:EOR01399.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR01399.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE007230; EOR01399.1; -; Genomic_DNA.
DR RefSeq; XP_009267661.1; XM_009269386.1.
DR AlphaFoldDB; R9AGP2; -.
DR STRING; 1299270.R9AGP2; -.
DR GeneID; 20377137; -.
DR KEGG; wic:J056_004185; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000014064; 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; 1.
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; 1.
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:UP000014064};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 55..485
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 849..968
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 776
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1031 AA; 111866 MW; 5575F68D3C46388E CRC64;
MLRSGALTSL RSLRSLRCRT STTSQCLRSL ATFEVADAPP TTANSIFAPL DSFTRRHVGP
RSAHVDQMLD SLGYTSFDHF INDAVPANIR IHDSINDSSI PPLSESELLA RAKQLGSQNK
LFKSYIGMGY HNAVTPPIIL RNITENPAWY TSYTPYQPEI SQGRLESLLN YQTMVSSLTG
MDIANASLLD EATAAAEAMV IAFGTAKGSK RTFIVDSGVL PQTLAVLHTR ARGLGINVVH
GDINDLLQKD NIRSDLVGAL FQYPNIDGAI QDYSNLISQV HSLSGLAVCA TDLLALTLLK
PPGEFGADIC VGNSARFGVP LGYGGPHAAF FACSDALKRR MPGRLIGVSK DSDGKIAYRL
ALQTREQHIR RDKATSNICT AQALLANMAA MYAVYHGPQG LRQIAAKVHA LTKVLKLGIE
KEGFTVKNRD SYFDTLTVHV ASAESTHAAA IANGINLRRV DDHTVGITLD ESVTEKDILT
LLDVFSQART ARGIEASQAA KDLTRPQALE EIALDLNLTR HTLPTLQVAA DEKLQRQSSY
LQHETFNRYQ SETELLRYIY YLQGKDLSLV HNMIPLGSCT MKLNSTSSMI PFTQPEWSSV
HPFVPIDQAQ GYAKMIRELE DDLAAITGFS ATSLQPNSGA QGEFAGLSVI KAYHESKGDG
GKRNICLIPL SAHGTNPASA VMAGMKVVPI KTLKDGRLDM EDLRGKCEEY SENLAAFMVT
YPSTFGVFEE GVQEACKLVH DKGGQVYLDG ANLNAQVGLT NPYTCGGDVC HLNLHKTFSI
PHGGGGPGVG PICVAEHLVP FLPGHPLSPH GTDSSLTPVS AAAQGSASIL TISWAYIKML
GGSGLTESSK IALLNANYIK KRLEGHFNVR FVNSKGAVAH ELLLDLANFE ESGLKVMDFA
KRLQDFGVHP PTCSWPITSA MLIEPTESEN KETLDRFIDA LIHIKGEADE VANGKADRVL
NVIKNAPHTL SSLAWSDDKW AATRPYSRQK AVYPLAYLAN NKFWPSVGRV DDAYGDRNLT
CSCPSVEEMA E
//
