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Database: UniProt
Entry: A0A1S2MXE4_9MICO
LinkDB: A0A1S2MXE4_9MICO
Original site: A0A1S2MXE4_9MICO 
ID   A0A1S2MXE4_9MICO        Unreviewed;       337 AA.
AC   A0A1S2MXE4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:OIJ34609.1};
GN   ORFNames=BK819_03800 {ECO:0000313|EMBL:OIJ34609.1};
OS   Microbacterium sp. LCT-H2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1914306 {ECO:0000313|EMBL:OIJ34609.1, ECO:0000313|Proteomes:UP000179624};
RN   [1] {ECO:0000313|EMBL:OIJ34609.1, ECO:0000313|Proteomes:UP000179624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCT-H2 {ECO:0000313|EMBL:OIJ34609.1,
RC   ECO:0000313|Proteomes:UP000179624};
RA   Huang B.;
RT   "Draft genome sequence of strain LCT isolated from the Shenzhou X
RT   spacecraft of China.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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:OIJ34609.1}.
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DR   EMBL; MODW01000001; OIJ34609.1; -; Genomic_DNA.
DR   RefSeq; WP_071327923.1; NZ_MODW01000001.1.
DR   AlphaFoldDB; A0A1S2MXE4; -.
DR   OrthoDB; 4324715at2; -.
DR   Proteomes; UP000179624; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd12167; 2-Hacid_dh_8; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          47..328
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          121..297
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   337 AA;  35506 MW;  72CBC7A4FFA4FAE2 CRC64;
     MTAGTSAPTV VAACSAELFA EFFSAEDAAR LETVAARLGG TFARVDRLAD AVLDEARVVV
     TSWGVGPFDH AVLATLPKLE LIAHTGATIK PFATDALFDR GVRVTQAGAG MARSVAEVSL
     TFTLALLHRV PEMHDALRAG DGWWDAEAVG VQHEILGAPV AVIGASRTGR AYLDLLRALG
     AEPLLVDPTL DAAEASSLGA ELVTLDEALR RAQIVAVHAP TLPETHHLIG ARELALMPDG
     AGLVNTARSW LVDEAALLAE LRRGRLSAAI DVFDEEPLSA ESPFRSAPRV LLTPHRAAGT
     REGRLRQGRI VADELDAFAA GRPLVHAVDR AQLSSMA
//
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