ID J9VU52_CRYNH Unreviewed; 1047 AA.
AC J9VU52;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CNAG_01594 {ECO:0000313|EMBL:AFR97798.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR97798.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR97798.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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}.
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DR EMBL; CP003830; AFR97798.1; -; Genomic_DNA.
DR RefSeq; XP_012052627.1; XM_012197237.1.
DR AlphaFoldDB; J9VU52; -.
DR GeneID; 23885292; -.
DR KEGG; cng:CNAG_01594; -.
DR VEuPathDB; FungiDB:CNAG_01594; -.
DR HOGENOM; CLU_004620_3_2_1; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000010091; Chromosome 11.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 76..520
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 869..989
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 33..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 713..740
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 796
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1047 AA; 113485 MW; E62A55FF5EDC3248 CRC64;
MSVSILRRAA RLPLSRQHQP LFARSLSISS IVLRPTSTSP TRSSTTATQP HPRSPSESFH
PAPTSVFTPL DTFLPRHLGP READIQAMLE VLGHKTLDEF VATTIPSQVR IDQLTNREEK
GKGLRALSEL ELRRRVEEVA AMNKPVKSYI GMGYHNAIVP PVIQRNVFEN PAWYTAYTPY
SPEQSQGRLE SLINFQTVAI SLTGLPIANA SLLDEGTAAA EAMAMCLASV AKPKFNKGKK
VFLVSPNVAP QTIEVLQTRA GGFDIDLRIA KSDANFLSEV ESLGEAQLMG ALVQYPDVNG
EIGDWEEVAT KVKATGAKMV VTSDLLALTM IKPPGEWGAD IVCGNSQRFG VPAGYGGPHA
AFFACTDDLK RKMPGRLVGL SKDSQGAPAY RLALQTREQH IRREKATSNV CTAQALLANM
AAMYAVYHGP EGLRRIAGKV HSLTRVLSES LASLGFTTVN KTFFDTLTID VSSAGVTAAD
VHAASVNAGI NFRKIDDKTI GITLDESVGP LDLTDIVNVF YAVKGQPAVE PEVLDALAQK
LELSAENVTS PIATLARTTP FLTQPVFNKH HSETDMLRYM MHLQEKDYSL VHGMIPLGSC
TMKLNSTSSM VPLSWKEFGG LHPFAPTDQA KGYEVIIKEL ENDLSLVTGY DATSVQPNSG
ASGEYAGLRV IQAYHESRGE GHRDVCLIPL SAHGTNPASA AMVGYKVVPI KALNDGSLDL
ADLKEKAEKH KDKLAAFMVT YPSTFGVFEE GIEEACQTVH DNGGQVYVDG ANCNSLIGLT
SLGRVGGDVS HTNLHKTFSI PHGGGGPGVG PISCKSHLAP FLPSHPIIPT GGSTPITAVS
AAPYGSASIN TISWAYIKML GGEGLTTVSK IALLNANYIA ERLKPYYNVR YSNKNGRVAH
ECLIDLAEFE KSADLKVPDF SKRLQDYSFH PPTAQWPIST CWLIEPTESE SKEEIDRFIE
ALISIRKEID EIVSGEQSKE DNVFKNAPHP LNLLTADKWD RPYSREKAVF PVPGLKKSKF
WPSVGRLDDA AGDLNLICEC GSVEEYA
//
