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Database: UniProt
Entry: A0A0V0UMA6_9BILA
LinkDB: A0A0V0UMA6_9BILA
Original site: A0A0V0UMA6_9BILA 
ID   A0A0V0UMA6_9BILA        Unreviewed;       529 AA.
AC   A0A0V0UMA6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   ORFNames=T09_12671 {ECO:0000313|EMBL:KRX52409.1}, T09_3373
GN   {ECO:0000313|EMBL:KRX52411.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52409.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX52409.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX52409.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX52409.1}.
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DR   EMBL; JYDN01000249; KRX52409.1; -; Genomic_DNA.
DR   EMBL; JYDN01000249; KRX52411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0UMA6; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:InterPro.
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; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        493..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          11..421
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
SQ   SEQUENCE   529 AA;  59534 MW;  9D63CAD46579F5F0 CRC64;
     MSSGMPLKYT RSLDELTDKA IPESIRLKKN LQLPKELGEE EALKRIKEIA SKNKIWKSYI
     GMGFNDCIIP SVIRRNVFEN LNWLTPYTPY QPEISQGRLE SLMNYQTMVC QMTSMDVSNA
     SLLDEATACA EAMQLCFSAT KNKIFFVDAY LHPQNIAVCS TRAQTMGIQL KLVRNWEKEN
     LDGISGAIVQ YPNTEGALVD YSALADRVHS HGGLFVMATD LLACALIRPP GEYKADVCVG
     NTQRFGLPLG YGGPHSAFFA VSNRFKNGAL IRLIPGRIVG LSKDRNGSPA YRLALQTREQ
     HIRRGKATSN ICTSQALLAN LSAMYAIHHG PGGLKRVAKK VHDATLVVAE GLKKCGFQLK
     HDNFFDTLTI ENIDSNQVEK IRRRAEQSHI NLRYYTNPNQ IGISLNETVE KEDLVNLLEI
     FDFKYDQHFK LNTIEANSVY HSNFARQSAF LTSDIFNSIH SEQMFVRYIE QLQSRDVSLV
     DSAIPLVENM QTIYLYILSI FGVFPFLTAS ISGFLHNEVE QFNTIDGEF
//
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