ID A0A443I629_BYSSP Unreviewed; 1062 AA.
AC A0A443I629;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=C8Q69DRAFT_29225 {ECO:0000313|EMBL:RWQ99553.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ99553.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ99553.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ99553.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
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:RWQ99553.1}.
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DR EMBL; RCNU01000001; RWQ99553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443I629; -.
DR STRING; 264951.A0A443I629; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000283841; 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 HAMAP; MF_00711; GcvP; 1.
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:UP000283841};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 81..542
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 562..834
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 883..1004
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 807
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1062 AA; 115962 MW; 83F716E4484AB8DC CRC64;
MAPSLYALRG ASNQLTRLSK LRVASTRALY RSPASSVASG RNYLQLRRHH ASARTVYTSS
LADYGEPEAR DLFQPIDTFP RRHIGPSPDA AKQMLATLDP PVASLDEFVQ QVLPADILSK
KDMVVTPPRV GTELQRDDVH GGLGETDMLK LLEKYRDQIT TTGKPYIGCG YYNTIVPPVI
LRNVLENPAW YTSYTPYQPE ISQGRLESLL NFQTLTADLT GLPVANASVL DEATAAAEAM
TMSLAVLPLA RQKKPGKVFV VSHLCHPQTI AVMRSRAEGF GIELKIGDIL ADDAKLVKDQ
GDSLIGVLAQ YPDTEGGIYD FESLGKTIHE LGGTFSVATD LLALTVLKSP GEFGADIAFG
SAQRLGVPMG FGGPHAAFFS CADKYKRKIP GRLVGVSKDR LGNRALRLAL QTREQHIRRE
KATSNICTAQ ALLANMSAMY AVYHGPKGLK AIAQRIMALT ALLQEKLTGL GYNVPTKSNV
SDGKAFFDTL TVELPNVDDA DAIMNAARSA NLYFRRLDIT RIGISLDETV GKNELKAILD
VFASHSSKAA VELSGELGPV AVPAALERTS SYLTHPVFNT HHSETEMLRY IHHLESKDLS
LAHSMIPLGS CTMKLNATSE MIPISWPEFS QMHPFTPTDA VAGYTQFIDE VEQQLADITG
MAEVTVQPNS GAQGEFTGLR VIKKYQDAQG GTRNVCLIPV SAHGTNPASA AMAGMRVVTI
KCDTKTGNLD IEDLKAKCEK HKDELAAIMV TYPSTFGVFE PGIKEVCKIV HEYGGQVYMD
GANMNAQIGL CSPGEIGADV CHLNLHKTFC IPHGGGGPGV GPIGVAEHLR PYLPSHPVSE
YLQGKRGDTA SPPVSAAPWG SASLLPITFN YINMMGAKGL THATKITLLN ANYILSRLKE
HYPILYTNEN GRCAHEFILD VRKFKETSGI EAIDIAKRLQ DYGFHAPTMS WPVANTLMIE
PTESENKAEL DRFCDALISI RQEIAAVERG EQPREGNVLK NAPHTQRDLL SSEWNRPYSR
EEAAYPQRWL LEKKFWPTVT RVDDAFGDQN LFCTCGPVED SE
//
