ID A0A016WS35_9BILA Unreviewed; 977 AA.
AC A0A016WS35;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN Name=Acey_s0553.g3357 {ECO:0000313|EMBL:EYC41848.1};
GN Synonyms=Acey-R12C12.1 {ECO:0000313|EMBL:EYC41848.1};
GN ORFNames=Y032_0553g3357 {ECO:0000313|EMBL:EYC41848.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC41848.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC41848.1}.
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DR EMBL; JARK01000153; EYC41848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WS35; -.
DR STRING; 53326.A0A016WS35; -.
DR Proteomes; UP000024635; 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:UP000024635};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 34..459
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 503..757
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 799..920
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 728
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 977 AA; 107830 MW; B5E120F723DE9316 CRC64;
MQRCVLGGAA TALRAFRATP RISARMVRYD AFADRHIGPS RLEKQQMLDF LGFTTLDELT
NTNVPNQIKL EREMDLPKPI DEYSMLRELK KIAEMNKIYR SYIGMGYYDT IVPAVILRNI
TQNIGWISQY TPYQAEISQG RLESLLNFQT MVADLTGLPS TNASLLDEST AVAEAIALAA
RATRRHKALL DPYLHPQNID VAKTRSGPLG IDLGELSFES LKIDKDVAAV VVQYPDTEGR
IRNLDQLIAK AHENGTLVVL VCDLMALTLL KSPGDLGADI AVGSAQRFGV PLGYGGPHAG
FMAVKKDSKN TLGRMMPGRI IGVTRGANGE KAFRLALQTR EQHIRRDKAT SNICTAQALL
ANMSAMYAVY HGPKRILEIA RAIHKSTAFL ESELVKAGHS TAHKDYFDTL KVTVKDLAAF
KQRAEEKHMN FRYFADGTVG VSLDEATKPS DLLDLLYVFN GSTKLTEDEV ADIVPETASP
LIGNSEHART SVFLEHPIFN TYHSEAQLVR YMKRLENKDV SLVHSMIPLG SCTMKLNASS
QLIPITWDSF NGLHPFAPVS QAAGFQKLFS DVEKWLCEIT GYDNFSLQPN SGANGEYTGL
LTIRKYLNSL GQQKRNVCLI PTSAHGTNPA SASMANMKVV PVESDKHGNI NYKDLAAKAE
RFKDELAAIM VTYPSTHGVF ESSIRDVIDK VHEHGGQVYL DGANMNAQVG LCRPGDYGSD
VSHLNLHKTF CIPHGGGGPG IGPIGVKKHL APFLPGHPVI PVDGRTDGAV AGAPWGSASI
LPITWAYIRM MGHAGLKKAS QMAILNANYM ARRLEGAYRI VYKDEQGLVA HEFILDCKPF
KKSAGVDVVD IAKRLMDYGF HSPTMSWPVH DCLMIEPTES EDKGEMDRLV DALLAIREEI
AMIERGELDK QRNPLKMAPH TLAKVSSNDW DLPYSRELAA FPKPWCHHKT WPTTGRVDDQ
YGDKNLVCTC PPMEAYQ
//
