ID A5U0B4_MYCTA Unreviewed; 326 AA.
AC A5U0B4;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:ABQ72464.1};
GN Name=serA2 {ECO:0000313|EMBL:ABQ72464.1};
GN OrderedLocusNames=MRA_0736 {ECO:0000313|EMBL:ABQ72464.1};
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ72464.1, ECO:0000313|Proteomes:UP000001988};
RN [1] {ECO:0000313|EMBL:ABQ72464.1, ECO:0000313|Proteomes:UP000001988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988};
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000611; ABQ72464.1; -; Genomic_DNA.
DR RefSeq; WP_003898565.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U0B4; -.
DR SMR; A5U0B4; -.
DR KEGG; mra:MRA_0736; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_3_11; -.
DR Proteomes; UP000001988; Chromosome.
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 GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001988}.
FT DOMAIN 43..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 34439 MW; DC0DA92C9B43012A CRC64;
MTPRPRALVT APLRGPGFAQ LRRLADVVYD PWIDQRPLRI YSAEQLADRI TAVAADVLVV
ESDSVGGPVF ERGLRVVAAT RGDPSNVDIP GATAAGIPVL HTPARNADAV AEMTVALLLA
VARHLIPADA DVRSGNIFRD GTIPYQRFRG AEIAGLTAGL VGLGAVGRAV RWRLSGLGLR
VIAHDPYRDD AGHSLDELLA EADIVSMHAA VTDDTIGMIG AQQFAAMRDG AVFLNTARSQ
LRDTDALVDA LRGGKLAAAG LDHFTGEWLP TDHPLVSMPN VVLTPHIGGA TWNTEARQAR
MVADDLGALL SGNRPAHVVN PEVLGS
//
