ID A0A2T9ZAN4_9FUNG Unreviewed; 1165 AA.
AC A0A2T9ZAN4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
DE Flags: Fragment;
GN ORFNames=BB560_003920 {ECO:0000313|EMBL:PVV01656.1};
OS Smittium megazygosporum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133381 {ECO:0000313|EMBL:PVV01656.1, ECO:0000313|Proteomes:UP000245609};
RN [1] {ECO:0000313|EMBL:PVV01656.1, ECO:0000313|Proteomes:UP000245609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-DP-2 {ECO:0000313|EMBL:PVV01656.1,
RC ECO:0000313|Proteomes:UP000245609};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(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:PVV01656.1}.
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DR EMBL; MBFS01000916; PVV01656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9ZAN4; -.
DR STRING; 133381.A0A2T9ZAN4; -.
DR Proteomes; UP000245609; 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; 1.
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 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:UP000245609};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 83..513
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 689..806
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 858..979
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1025..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 782
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
FT NON_TER 1165
FT /evidence="ECO:0000313|EMBL:PVV01656.1"
SQ SEQUENCE 1165 AA; 127537 MW; 9D505764BD23DE17 CRC64;
MSSSKFSSFS KRFPNLKPAL NQYYRLNPRA LAVDSPHCRL FSVSTATAFK HSSVSAVDKS
YPPENATVAS KHAFFAPLDS FARRHLGPRE AEIPEMLKTV GVSSIDEMVN KVIPSHILAK
HNLIIENGGL SEQEMLSYLK SIAKQNKVYK SYIGMGFNDT IMPPVIQRNI LENPGWYTQY
TPYQPEISQG RLESLLNFQT AVQDFTGMPI ANASLLDEGT AAGEALAVCV SSSKKKSNLY
FFVDENCHPH TVAVVKTRAS GLNVSVIVGN FESFDFNSSH GNLIGALVSY PDTFGNISNF
KQFADQVHSN GAQFVVSADI MALAVLEPPS TFGADIVVGN TQRFGVPLGY GGPHAAYFAT
TEANRRRIPG RIIGVSKDSK GRQAYRLALQ TREQHIRREK ATSNICTAQA LLANIASMYA
VYHGPQGIKD IANRIHRYTA VLASVLQGAG YKVENTSFFD TIKVNVNPED SAQVIQRAAN
IGINFRQIGN DHVGISIGES VTLEDLGAIV SVFKTDLNNI DTLVQNLPLD TSSSKFIPSE
LIRKSPFLTH PIFSKYHSET EMLRYLTQLQ NKDLSLANAL IPLGSCTMKL NATSQMIPIT
WPEFSDIHPF APKDQALGYK KLIHEIELDL ARITGMDGTS VQPNSGAQGE YTGLRVIKKY
HESIGEGHRN ICLIPVSAHG TNPASAMMAN LKVVTVKCES NGYLDIDDLK LKIQKHAANL
SSVMITYPST FGIFEEKIIE ITNLVHENGG QVYMDGANMN AQIGLMNPGE IGADVCHLNL
HKSFCIPHGG GGPGVGPICV KKHLIPFLPT DSLMESNLDA VANQSVGPST SAPYGSAGIL
PISWAYIKLM GGAGLRKSTE VAILNANYMM RRLESHYLVQ YTNSNNMCAH EFILDLHEFS
KSAGVSVVDI AKRLQDYGIH PPTMSWPVPN GLMIEPTESE SLFEIDRFCD AMIQIRNEIR
DIEQGKYPRD NNLLVNSPHS LEDIASDTWN HPYSREQAAY PLKSLRARKF WPTISRIDDT
YGDTNFKKSI SNDSGKKSTT KTKAEATKSS TSAHIQVINT EVALSNTAEL MMQQNNIDEM
EVELFLNEVK QEMTAEIASN PESAGLNTPQ IINITGDLAD CTTSVATDTV HATVNTASTV
VYNGQSSKGD TGHEKIEVVS SPAIK
//
