ID A0A0L6U4U2_9FIRM Unreviewed; 282 AA.
AC A0A0L6U4U2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glycine cleavage system protein H {ECO:0000313|EMBL:KNZ43549.1};
GN ORFNames=AKG39_00465 {ECO:0000313|EMBL:KNZ43549.1};
OS Acetobacterium bakii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ43549.1, ECO:0000313|Proteomes:UP000036873};
RN [1] {ECO:0000313|Proteomes:UP000036873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT psychrophilic chemical producer through syngas fermentation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvH family.
CC {ECO:0000256|ARBA:ARBA00009249}.
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:KNZ43549.1}.
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DR EMBL; LGYO01000002; KNZ43549.1; -; Genomic_DNA.
DR RefSeq; WP_050738392.1; NZ_UOGO01000001.1.
DR AlphaFoldDB; A0A0L6U4U2; -.
DR STRING; 52689.AKG39_00465; -.
DR PATRIC; fig|52689.4.peg.848; -.
DR OrthoDB; 9796712at2; -.
DR Proteomes; UP000036873; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
DR CDD; cd06848; GCS_H; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR014958; DGC.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR00527; gcvH; 1.
DR PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR PANTHER; PTHR11715:SF3; GLYCINE CLEAVAGE SYSTEM H PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF08859; DGC; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000036873}.
FT DOMAIN 170..252
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 211
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 282 AA; 31280 MW; 8E06C1DD0DC1DC31 CRC64;
MSKTICVLPC NGLDKCAGDV SRRVALQLAQ SDAVELICPV LLNQNKSRYE KVLESGELTV
IDGCNTRCAS KLAGDLELFI KEKVNVSEVA KALNIKLGVE IREDEDSKAV VQEVLEKISS
SVAVQAESEF IEPESVAYDS FSHGKFIFKI PKSNYFFNEN DCWVTVSGNM ARIGVSDYVQ
QNLSDILYVD PPEIGDEFEQ FDDLGSIESG KAVFEIISPV SGTVVAVNTA LSDAPELVNE
SPYEKGWLVE VRLSDFEEDQ DLLHDCPTYF KFLQRKVEEV DV
//
