ID C4JGC6_UNCRE Unreviewed; 1061 AA.
AC C4JGC6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=UREG_02524 {ECO:0000313|EMBL:EEP77675.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP77675.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476615; EEP77675.1; -; Genomic_DNA.
DR RefSeq; XP_002543008.1; XM_002542962.1.
DR AlphaFoldDB; C4JGC6; -.
DR STRING; 336963.C4JGC6; -.
DR GeneID; 8443212; -.
DR KEGG; ure:UREG_02524; -.
DR VEuPathDB; FungiDB:UREG_02524; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR InParanoid; C4JGC6; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000002058; 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 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:UP000002058};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 80..536
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 557..830
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 882..1003
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 51..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 805
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1061 AA; 115308 MW; 2D1D56EB3C63AB67 CRC64;
MVAPFAVLRT GARQLAYNSL RNAALRSSRV SPLTACRQCL QLSRFQQTQS ARRAVHSSSG
ADTDSLQPRD LLSPLDTFPR RHIGPGADAT EQMLGALDPP AKSLDEFVQQ VLPGDILTAR
NLSVTEPKSA AGLRKDGVLG GLGEKDMIKL LESYKAKIDA TGKSFIGCGY YSTVVPPVIQ
RNVLENPAWY TSYTPYQPEI SQGRLESLLN FQTLTADLTG LPVANASVLD EGTAAAEAMT
MSWATLPMSK QKQDGKVFVV SHLCHPQTIA VLRSRAEGFG IRLEIGDIMA EDFKLVKGQG
DRLIGVLAQY PDTEGAVLDF ENLSNQIHAQ GGTFSVATDL LALTVLKAPG EFGADIAFGN
AQRLGVPMGF GGPHAAFFAC TDKYKRKIPG RIVGVSKDRL GNRALRLALQ TREQHIRREK
ATSNICTAQA LLANMTAMYA VYHGPKGLKA IAERIMALTT LLRQNLELLG FNVLARGNAF
FDTLTIEAKD ASEADSIVTS ALNSGLYLRR VSPTKVGISL DESVGVDELK ELLSVFASIS
SKGGAEVLNV KDVPSIELPA SVKRTSSYLT HPVFNTHHSE TEMLRYMQHL VSKDLSLAHS
MIPLGSCTMK LNATTEMVPI TWPEFSTMHP FTPAQKVEGY VDMVEDLEQQ LADITGMAEV
TIQPNSGAQG EFAGLRVIKK YQDSIGEPGK RNICLIPVSA HGTNPASAAM AGMKVVTVKC
DTATGNLDLA DLRVKCQKHK DELAAIMVTY PSTFGVYEPT IKEVCNIVHE HGGQVYMDGA
NMNAQIGLCS PGEIGADVCH LNLHKTFCIP HGGGGPGVGP IGVAEHLRLF LPSHPLSEPL
LAKRSSSVDS PPISAAPFGS ASILPITFSY INMMGSKGLT HATKITLLNA NYLLSRLKPH
YPILYTNTNG RCAHEFILDV RKFKATAGVE AIDIAKRLQD YGFHGPTMSW PVANTLMIEP
TESEPKAELD RFCDALISIR EEIAAIERGE QPRENNVMKM APHTQRDLLA TEWDRPYTRE
KAAYPLPWLL EKKFWPTVTR VDDAFGDQNL FCTCGPVEDS E
//
