ID R9MTL6_9FIRM Unreviewed; 522 AA.
AC R9MTL6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EOS74026.1};
GN ORFNames=C817_04872 {ECO:0000313|EMBL:EOS74026.1};
OS Dorea sp. 5-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1235798 {ECO:0000313|EMBL:EOS74026.1, ECO:0000313|Proteomes:UP000014211};
RN [1] {ECO:0000313|EMBL:EOS74026.1, ECO:0000313|Proteomes:UP000014211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:EOS74026.1,
RC ECO:0000313|Proteomes:UP000014211};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Dorea bacterium 5-2.";
RL Submitted (APR-2013) 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 -!- 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:EOS74026.1}.
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DR EMBL; ASTD01000097; EOS74026.1; -; Genomic_DNA.
DR RefSeq; WP_016221502.1; NZ_KE159721.1.
DR AlphaFoldDB; R9MTL6; -.
DR STRING; 1235798.C817_04872; -.
DR PATRIC; fig|1235798.3.peg.5130; -.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_5_0_9; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000014211; 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 Gene3D; 6.20.440.10; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000014211}.
FT DOMAIN 178..297
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 371..474
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
SQ SEQUENCE 522 AA; 58375 MW; 75F52E95D2B5DE95 CRC64;
MGYVKKNRDF HEARWDEPFI MEMGNPGERG VLIPRASEGV QRVSGSAADL IPAGLRRKKA
PKLPEVSQMQ VLRHYMRLSQ ETIGTDLNID IGLGTCTMKY SPKIHEQLVR SEKFQELHPC
QDESTVQGIL EIMYQDAQYL KAISGMDQVS LQPAGGSQAI FANVQAIRAY FEKKGEGGQR
DEIITTILSH PANPGTAATL GYKVITLYPD ENGLPDIEAL KAAVSEHTAA LMITNPEDTG
IYNDRIRQFV DIVHEAGGLC VYDQANLNGV FGLTRARDAG FDMCHYNLHK SFSSPHGCQG
PGAGAQCVSK ELAGYVAAPV VEFDGTRYYL DHQMPDSIGK LRSFYGVPSV MIRAYAYIRS
LGADGMRQIA ELSILNNNYL ISRLLKIRGL TMPFAEGRFR MEQARLSWQE LTEETGVTTD
DICRRIVDYG FQDYFTSHHP RVLPEPFTPE PVETYSKDDM DEYVAAFEAI SQEAYTDPEL
VKGAPYKAAL GARIEEECLT DWSRFATTWR AYKRMEGEEI LC
//