ID G7XJD7_ASPKW Unreviewed; 1060 AA.
AC G7XJD7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=AKAW_05276 {ECO:0000313|EMBL:GAA87162.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA87162.1};
RN [1] {ECO:0000313|EMBL:GAA87162.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA87162.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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; DF126458; GAA87162.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XJD7; -.
DR STRING; 1033177.G7XJD7; -.
DR VEuPathDB; FungiDB:AKAW_05276; -.
DR eggNOG; KOG2040; Eukaryota.
DR InParanoid; G7XJD7; -.
DR Proteomes; UP000006812; 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 78..539
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 552..832
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 881..1002
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 38..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..854
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 1060 AA; 115009 MW; B9139F1673D09A2A CRC64;
MAASLCALRG TRQLALRSRL RAAPSPIAVR RASPLIRSLH TTTQQSPSAR RPVYTSSVAD
HGVPHPPDLF QPLDTFPRRH IGPNPDAAKE MLATLDPPVA SLDEFVKQVL PADILSKKDL
KVSAPHSTAN LPHSSVHGGL GETDMLKLLD TYRKQIDVSG KTYLGTGYYP TIVPPVVLRN
VLENPAWYTS YTPYQPEISQ GRLESLLNFQ TLTADLTGLP FANASVLDEG TAAAEAMTMS
LATLPMSKQK KAGKAYVVSH LCHPQTIAVM RSRAEGFGIN LVVGDILADD FKLVKEQGDK
LIGVLAQYPD TEGGIYDFQS LSDTIHGNGG TFSVATDLLA LTLLKAPGEF GADIAFGSAQ
RLGVPMGYGG PHAAFFACAD KYKRKVPGRV VGVSKDRLGN RALRLALQTR EQHIRREKAT
SNICTAQALL ANMTAMYAVY HGPAGLKAIA QRIMSMTTTL QAKLAGLGYN VPIKSNSADG
GALFDTVVVE LSGAQETDAI IAAAREQSMF LRRLSDTKVG ISLDETVGRE EVKSILKVFA
AHASKAEVGL EEDLAVAPVP ASLERTSAYL THPVFNTHHS ETEMLRYIRH LESKDLSLAH
SMIPLGSCTM KLNATTEMIP VSWPEFSQMH PFLPADVAKG YTQMIDDLEQ QLADITGMAE
VTVQPNSGAQ GEFAGLRVIK KYQEAHEGDK RNICLIPVSA HGTNPASAAM AGMRVVTIKC
DTKTGNLDLE DLKAKCEKHK DELAAVMITY PSTFGVYEPG IKQACEIVHQ HGGQVYMDGA
NMNAQIGLCS PGEIGADVCH LNLHKTFCIP HGGGGPGVGP IGVAEHLRPY LPSHPGSEYL
QSKRSESSSP PISAAPWGSA SILPITFNYI NMMGSKGLTH ATKITLLNAN YILARLKDHY
PILYTNENGR CAHEFILDVR KFKDTCGVEA IDIAKRLQDY GFHAPTMSWP VANTLMIEPT
ESENKAELDR FCDALISIRE EIAAVESGAQ PQEGNVLKMA PHTQRDLLSS EWNRPYTRET
AAYPLPYLVE KKFWPSVTRV DDAYGDQNLF CTCGPVEDSE
//
