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Database: UniProt
Entry: B1MJX7_MYCA9
LinkDB: B1MJX7_MYCA9
Original site: B1MJX7_MYCA9 
ID   B1MJX7_MYCA9            Unreviewed;       314 AA.
AC   B1MJX7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=NAD-binding protein (D-isomer specific 2-hydroxyacid dehydrogenase?) {ECO:0000313|EMBL:CAM64484.1};
GN   OrderedLocusNames=MAB_4414 {ECO:0000313|EMBL:CAM64484.1};
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS   104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS   abscessus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM64484.1, ECO:0000313|Proteomes:UP000007137};
RN   [1] {ECO:0000313|EMBL:CAM64484.1, ECO:0000313|Proteomes:UP000007137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC   TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CU458896; CAM64484.1; -; Genomic_DNA.
DR   RefSeq; WP_005089422.1; NZ_MLCG01000001.1.
DR   AlphaFoldDB; B1MJX7; -.
DR   GeneID; 66969847; -.
DR   KEGG; mab:MAB_4414; -.
DR   Proteomes; UP000007137; 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   CDD; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          37..305
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..273
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   314 AA;  34287 MW;  AC2C71C15AEFBD3E CRC64;
     MNEQLVRRPV IAVQHSPDSV PERLAPVTAA AEVRLVESDR LATALPGAEV LFVYDFRSSA
     LRETWSAADS LRWVQIASTG VDPVLFDEFV ASDVVLTNSR GIFERPIAEY VLAQILAFAK
     DIRRSTRAQA ALSWRHFESE SIEGTPVGVL GTGPIGQAIS TLLGAVGMRV TVLGRAESAD
     LSSHVGEFEY LVLAAPLTPQ TRGIVNARVL SAMRPTARLI NVGRGELVGT WDLVSALNRG
     GIAGAALDVT DPEPLPVGHP LWRTPNTHIT PHNSGDVRGW SDRLQDQFVV NFERYLRGEE
     LLNIVDKNRM HRHA
//
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