ID R7JPT0_9BACT Unreviewed; 809 AA.
AC R7JPT0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=BN752_00946 {ECO:0000313|EMBL:CDE64877.1};
OS Alistipes putredinis CAG:67.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1263036 {ECO:0000313|EMBL:CDE64877.1, ECO:0000313|Proteomes:UP000018026};
RN [1] {ECO:0000313|EMBL:CDE64877.1, ECO:0000313|Proteomes:UP000018026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:67 {ECO:0000313|Proteomes:UP000018026};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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 -!- 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:CDE64877.1}.
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DR EMBL; CBJI010000076; CDE64877.1; -; Genomic_DNA.
DR Proteomes; UP000018026; Unassembled WGS sequence.
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); 2.
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; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018026}.
FT DOMAIN 7..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT REGION 685..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 88978 MW; 0057690DD96C31C2 CRC64;
MFDKFSDRHI GVTNPEDLKA MLAVIGVKSV DELIAQVIPQ SIRLKQPLAL PQGMSEYEFA
NHIQALAAKN RTLRSFIGMG YYPCAVPAAI TRNVFENPAW YTSYTPYQAE ISQGRLEALL
NFQTAVISLT GMEIGNCSLL DEGTAAAEAM LMMFSLRSRE AVKEGRNQLF VDRNIFPQTL
DVLITRSEPF GIELVIDDYN TYEFTGKEFG AIVQYPAANG EVRDYAAFTE AAHAKGALVT
AVADLLSLAL LKAPGEWGAD IVVGTTQRLG IPMGFGGPSA GYMTTREAYK RNMPGRIIGV
SIDRLGNRAL RMALQTREQH IKRERATSNI CTATALMASM VGFYCVYNGA EGLRRSAKTA
HTAAVTVAKA LEAMDYKLAA KNFFDTLEVE AEAAVVQSLA LERGINFFYP SEDRVRFSFD
DVTTPEEVNE VIAIFAEAKG KKAKAVKLSE EITIPAAILR QSEFLTERVF NTYRCESDLM
RYIKRLELRD ISLANSMISL GSCTMKLNAA ALMQPLSLAG FQNMHPFAPA DQTEGYRELI
DGLAADLATI TGFAACSLMP NSGAAGEYTG LMVIRAYHQS RGQGYRNIVL IPSSAHGTNP
ASAAMAGMKI VTVGCDANGN IDVEDLKAKA QEHSSELACM MITYPSTHGV FESRIREIVD
AVHGGGGQGX XRGCRTRRRR TGIYGRCQHE RPGRPHEPRL HRCGRLPPEP AQDLRNASRR
RRPGRRSDLR GGAPPQVPPL AFDRPHRRRR RHHGRGIGTL GFGHALPDHL RLHQDAGRRR
SESGYRDGDR ERQLHVVGPQ IGVPHLLFG
//
