ID F2TNH7_AJEDA Unreviewed; 1074 AA.
AC F2TNH7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=BDDG_07735 {ECO:0000313|EMBL:EGE84790.1};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE84790.1};
RN [1] {ECO:0000313|EMBL:EGE84790.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE84790.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) 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}.
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DR EMBL; GG749476; EGE84790.1; -; Genomic_DNA.
DR AlphaFoldDB; F2TNH7; -.
DR HOGENOM; CLU_004620_3_2_1; -.
DR Proteomes; UP000007802; 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; 1.
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 Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 84..545
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 564..842
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 893..1014
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 816
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1074 AA; 116510 MW; 0110E5571EAE2C4A CRC64;
MAAPSSILLR GGGRRLARCY PRAEAASKVL RLSPLTACRQ CLKSATPRLL SSYSSRRYVH
SSSLSDQRTP QPRNLIQPLD SFPRRHIGPT PDTAEQMLAA LDPPVNSLDE FVKQVLPADI
VSARDLEIVK PDGSTGLHAD SVHGGLGESD MIKLLQKYAK DIDASGKPYI GCGYYNTVVP
PVIQRNVLEN PLWYTSYTPY QAEISQGRLE SLLNFQTVTA DLTGLPVANA SVLDEGTAAA
EAMTMSWATM PVQKQKKEGR SYVVSHLCHP QTIAVMQSRA EGFGIKLVVG DIMSEDFKLV
KDQGDCLIGV LAQYPDTEGG IYDFQSLSDK IHEIGGTFSV ATDLLALTLL KPPGEFGADI
AFGTAQRFGV PMGFGGPHAA FFACADKYMR KIPGRIVGVS KDRLGNRALR LALQTREQHI
RREKATSNIC TAQALLANMS AFYAVYHGPE GLKAIAQRIR SLTGLLREKL RALGYTVPVK
GNTASDGAIF DTLTVETGSS GEADSLMEVA LQSSIYLRRV NPTTIGVSLD ESVGVEELKG
LLSVFSKTAP KGAPADLLNI SEDVPELEIP ASVKRTSPYL THPVFNSHHS ETEMLRYITH
LGSKDLSLAH SMIPLGSCTM KLNATTEMVP ITWPEFSTMH PFTPSKIVTG YQKMIEDLEH
QLADITGMAE VTVQPNSGAQ GEFAGLRAIK MYQDSIGTPG KRNLCLIPVS AHGTNPASAA
MAGMRVLSIK GDPVSGNLDL ADLKAKCEKH KDELAAIMIT YPSTFGVFEE GVKEACKIVH
ENGGQVYMDG ANLNAQIGLC SPGEIGADVC HLNLHKTFCI PHGGGGPGVG PIGVAEHLRP
FLPSHPLSQH LQSRRSTSNP APPISAAPWG SASILPITFS YINMMGAKGL THATKITILN
ANYILSRLKP HYPILYTNAH GRCAHEFILD VRKFKATSGI EAIDIAKRLQ DYGFHAPTMS
WPVANTLMIE PTESESKAEL DRFCDALIAI RGEIAAIEAG KQPREGNVLK MAPHTQRDLL
GAEEWNRPYT REQAAYPVPW LLEKKFWPSV TRVDDAFGDQ NLFCTCGPVD DTIE
//
