ID B8H8B8_PSECP Unreviewed; 319 AA.
AC B8H8B8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:ACL38092.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:ACL38092.1};
GN OrderedLocusNames=Achl_0089 {ECO:0000313|EMBL:ACL38092.1};
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL38092.1, ECO:0000313|Proteomes:UP000002505};
RN [1] {ECO:0000313|EMBL:ACL38092.1, ECO:0000313|Proteomes:UP000002505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001341; ACL38092.1; -; Genomic_DNA.
DR RefSeq; WP_012630828.1; NC_011886.1.
DR AlphaFoldDB; B8H8B8; -.
DR STRING; 452863.Achl_0089; -.
DR KEGG; ach:Achl_0089; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_11; -.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000002505; Chromosome.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05301; GDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 124..291
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
SQ SEQUENCE 319 AA; 33615 MW; 47BF326EA3F09070 CRC64;
MSRVVVTGRI PEAAIEKLRA EHEVDVWEGP ESISREELLR RVAGADGIVS LLTERVDAEL
LDAAGPQLKV VANVAVGYDN IDVPACTERG VIATNTPGVL TDATADIALS LILMATRRLG
EGERLIRSGE AWKWGMFFLL GSSLQGKTLG VVGMGGIGQA TARRAKAFGM EIVYQSRSEI
DPAIAGELGA RRVELDELLA ISDVVSLHCP YGPATHHLIG AEQLAAMKDS AFLVNTARGP
IVDEAALAAA LRDGRIAGAG LDVYEKEPQV HPGLLGLDNV VLLPHLGSAT VETRTAMAML
AADNALAVLS GERPATPIR
//
