ID I0IL30_LEPFC Unreviewed; 503 AA.
AC I0IL30;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN OrderedLocusNames=LFE_0257 {ECO:0000313|EMBL:BAM05979.1};
OS Leptospirillum ferrooxidans (strain C2-3).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM05979.1, ECO:0000313|Proteomes:UP000007382};
RN [1] {ECO:0000313|EMBL:BAM05979.1, ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|EMBL:BAM05979.1,
RC ECO:0000313|Proteomes:UP000007382};
RX PubMed=22815442; DOI=10.1128/JB.00696-12;
RA Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA Kamijo T., Ohta H.;
RT "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT Japan.";
RL J. Bacteriol. 194:4122-4123(2012).
RN [2] {ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA Kamijo T., Ohta H.;
RT "The complete genome sequence of the pioneer microbe on fresh volcanic
RT deposit, Leptospirillum ferrooxidans strain C2-3.";
RL Submitted (MAR-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};
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DR EMBL; AP012342; BAM05979.1; -; Genomic_DNA.
DR RefSeq; WP_014448472.1; NC_017094.1.
DR AlphaFoldDB; I0IL30; -.
DR STRING; 1162668.LFE_0257; -.
DR GeneID; 78148125; -.
DR KEGG; lfc:LFE_0257; -.
DR PATRIC; fig|1162668.3.peg.298; -.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_5_0_0; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000007382; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR Gene3D; 6.20.440.10; -; 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; 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 InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007382}.
FT DOMAIN 158..288
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 364..459
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 53314 MW; C9FC26C9D7AA3559 CRC64;
MTIRANSEER SARPDMHPTL WEISRPGARG VFPPSVSGST DFGVPEVSMR DSPPCLPELS
ELEVVRHFTN LSHLSRGVDT HFIPLGSCTM KYNPKVSDKV ASLPGFSDLH PRTDPEGMEG
LLEAMGTLSD LLKSLLGMDA VTLAPAAGAH GELTGILIAR KYFESRGETS RKVILVPDSA
HGTNPASASM GGMVVRSITS KPSGHIDTAA LEKALSSETA MVMITAPSTL GLFEEELSEV
VRLVHKAGAL VYMDGANMNA FLGVLKPGDL GFDIVHINTH KTLATPHGGG GPGSGPVGVK
SHLAPFLPTP VIVKMNHVYS FANPEDSSSI GPVRSFLGST GVLLRALSYV LLLGREGLPR
VALYALLNAN YLKKKLDGVL PGEGPGLCAH EFVLSAKPLA AFGVHAGDLA KGLLDAGYYA
PTIHFPLIVP EALMIEPTEC ESKSMLDAFA EDFSRIVEKA ALHPSEILSA PLRTPVSRPD
EVLAARDPVL KDPTVSSGNL RKD
//
