ID I9S3K9_9BACE Unreviewed; 948 AA.
AC I9S3K9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=HMPREF1068_02367 {ECO:0000313|EMBL:EIY49808.1};
OS Bacteroides nordii CL02T12C05.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997884 {ECO:0000313|EMBL:EIY49808.1, ECO:0000313|Proteomes:UP000003089};
RN [1] {ECO:0000313|EMBL:EIY49808.1, ECO:0000313|Proteomes:UP000003089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C05 {ECO:0000313|EMBL:EIY49808.1,
RC ECO:0000313|Proteomes:UP000003089};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides nordii CL02T12C05.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein. {ECO:0000256|ARBA:ARBA00003788}.
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 ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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:EIY49808.1}.
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DR EMBL; AGXS01000016; EIY49808.1; -; Genomic_DNA.
DR RefSeq; WP_007485463.1; NZ_JH724314.1.
DR AlphaFoldDB; I9S3K9; -.
DR STRING; 997884.HMPREF1068_02367; -.
DR PATRIC; fig|997884.3.peg.2430; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_10; -.
DR Proteomes; UP000003089; 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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000003089}.
FT DOMAIN 9..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 476..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 772..893
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 704
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 948 AA; 105165 MW; AF98E94CD77A48D4 CRC64;
MKTDSFASRH IGVSEKDIEV MLRKIGVSTL DELIDKTIPA NIRLKEPLAL PPAMTEYEFS
KHIAELAGQN KLFTTYIGMG WYNTITPAVI QRNVFENPVW YTSYTPYQAE VSQGRLEALM
NFQTVVCDLT AMPLANCSLL DEATAAAEAV TMMYGLRPRD KQKLGANVVF VDENIFPQTL
AVMNTRAIPQ GIELRVGKYQ EFEPTPEVFA CILQYPNSDG SIEDYRNFTE KAHEADCKVA
VAADLLSLAL IVPPGEWGAD IVFGTTQRLG TPMFYGGPSA AYFATRDEFK RNMPGRIIGW
SKDKYGKMCY RMALQTREQH IKREKATSNI CTAQALLATM AGFYAVYHGQ QGITDIASRI
HSISAFLEKE ISKLGYKQVN KYYFDTLRFI LPDNVSAPQV RTIALSKEVN LRYFDNGDVG
FSIDETTDIS AANMLLSIFA IAAEKDYQKI TEIPDADTFS KELKRQSAFL THEVFNKYHT
ETEMMRYIKR LDRKDISLAQ SMIPLGSCTM KLNAAAEMLP LSRPDLLCMH PLVPEDQAEG
YRKLIENLSD ELKIITGFAG VSLQPNSGAA GEYTGLRVIR SYLESIGQGH RNKILIPASA
HGTNPASAIQ AGFTTITCAC DEHGNVEMND LRAKAEENKE ELAALMITYP STHGIFETEI
VEICDIIHAC GAQVYMDGAN MNAQVGLTNP GFIGADVCHL NLHKTFASPH GGGGPGVGPI
CVAEHLIPFL PGHGLFGNPI NEVSAAPFGS AGILPITYGY IRMMGTEGLT MATKTAILNA
NYLAACLKDT YGIVYRGANG FVGHEMILEC RKVHEETGIS ENDIAKRLMD YGYHAPTLSF
PVHGTLMIEP TESESLWELD NFVTVMQTIW KEIQEVKNGE ASAEDNVLIN APHPEYEIVN
DHWEHSYTRE KAAYPIESVR ENKFWVNVAR VDNTLGDRKL LPTRYGSF
//
