ID G1X386_ARTOA Unreviewed; 1118 AA.
AC G1X386;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=AOL_s00043g159 {ECO:0000313|EMBL:EGX52370.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX52370.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX52370.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EGX52370.1}.
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; ADOT01000057; EGX52370.1; -; Genomic_DNA.
DR RefSeq; XP_011118948.1; XM_011120646.1.
DR AlphaFoldDB; G1X386; -.
DR STRING; 756982.G1X386; -.
DR GeneID; 22889841; -.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_3_2_1; -.
DR InParanoid; G1X386; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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; 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 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; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT DOMAIN 100..544
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 930..1051
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 35..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 123604 MW; A1C466103A527FBE CRC64;
MTTLLARSAR ITLPTRHLLA ARLPATAVRR CFSDQTAPDD SASKVENSAE NLKLPPKQKE
RKTYPLPKIE LPFMKEDLVF NGQTNLTAPE PLTDLDTLPR RHIGPDPNEI KQMLDTIGVK
SMEEFIHSVV PEQIRSGQDL KVSQKYGLSE TLWQTRFKEI IASITTTYSF VGQGYYGTKV
PEVIKRNILE CPEWYTSYTP YQAEISQGRL ESLINFQTMV TSLTGLQIAN ASVLDELTAA
AEAMTFAYAC LSASRQKSTN KVFLVSNKMF PQTIDGLYPR AEGFNIKIVV ADLETANLDE
LIGDGDMIGA MVQYPDIDSN TGKWLPSFTE DIHARGGIVC CGTDLLALTM LKPPGEWGAD
VAFGSAQRFG VPMGLGGPHA GFFATSDKHK RKLPGRLIGA SKDRLGDKAY RLALQTREQH
IRREKATSNI CTAQALLANM SAMYAVYHGP GGLKKIAQKV VATRQIFAQA LLDIGWPQEL
VKESDFDTVH VGFSDPKTWK KMQTPSYMYA GELRSHKDGD QHWISVSFDE TTDWQRLSKL
IQLFNHIGPT KRDIAATKIG DEAEASDEAT KGAEEKKKNV YLLDQHSRSI ARTATEKVLG
TGNMGQVRAD FARESKFLEQ PVFNKYHSET EMLRYIHHLQ SKDLSLANTM IPLGSCTMKL
NATSEMIGLS FQKLGNLHPL TPARKLGYFP DMVKSLEKDL CVITGFDACS IQPNSGAQGE
FTGLRMIRNY LKSIGQGQRD TLLIPVSAHG TNPASATMVG FKVQPVKCDT KTGNLDLQDL
KAKAEKLGDK LAGAMITYPS TFGVFEPGVK DAIQIVHDNG GQVYMDGANM NAQIGITSPG
YLGADVCHLN LHKTFCIPHG GGGPGVGPVC VAKHLEPFLP SHTDSSNETL RPSATSSIGP
VSSAQYGSAS ILPISYSYIK MMGAVGLKHA TEICLLNANY MAKRLSDHYD ILYTNENGRC
AHEFILDPRP LKETSGVEAV DIAKRLMDYG FHAPTMSWPV PGTLMIEPTE SESKEEMDRY
CDALIEIRNE IREIEEGKMR KDVNVLKMAP HPMQDLLQGE EVWKDRGYTR EKAGYPLEYL
RERKFWPSVA RVDDAFGDTN LFCTCDPMPQ EGDAPAEH
//
