KORB_MYCTU
ID KORB_MYCTU Reviewed; 373 AA.
AC O53181; F2GHL5; L0TCK6;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=2-oxoglutarate oxidoreductase subunit KorB;
DE EC=1.2.7.3 {ECO:0000269|PubMed:19936047};
DE AltName: Full=Alpha-ketoglutarate oxidoreductase subunit beta;
DE Short=KG oxidoreductase subunit beta;
DE Short=KGO subunit beta;
DE Short=KOR subunit beta;
GN Name=korB; OrderedLocusNames=Rv2454c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, ROLE IN TCA CYCLE, GENE
RP NAME, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19936047; DOI=10.1371/journal.ppat.1000662;
RA Baughn A.D., Garforth S.J., Vilcheze C., Jacobs W.R. Jr.;
RT "An anaerobic-type alpha-ketoglutarate ferredoxin oxidoreductase completes
RT the oxidative tricarboxylic acid cycle of Mycobacterium tuberculosis.";
RL PLoS Pathog. 5:E1000662-E1000662(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Component of KG oxidoreductase (KOR) that catalyzes the CoA-
CC dependent oxidative decarboxylation of 2-oxoglutarate (alpha-
CC ketoglutarate, KG) to succinyl-CoA. Methyl viologen can act as electron
CC acceptor in vitro; the physiologic electron acceptor is unknown. Is
CC involved in the alternative TCA pathway that functions concurrently
CC with fatty acid beta-oxidation. Since a growing body of evidence
CC indicates that lipids (for example cholesterol and fatty acids) are a
CC predominant growth substrate for M.tuberculosis during infection, flux
CC through KOR likely represents an important step in intermediary
CC metabolism in vivo. KOR-dependent decarboxylation of KG also appears to
CC be an important source of CO(2) in M.tuberculosis metabolism.
CC {ECO:0000269|PubMed:19936047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2
CC + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + succinyl-CoA;
CC Xref=Rhea:RHEA:17297, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57292; EC=1.2.7.3;
CC Evidence={ECO:0000269|PubMed:19936047};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19936047};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000269|PubMed:19936047}.
CC -!- SUBUNIT: KG oxidoreductase (KOR) is composed of KorA and KorB subunits.
CC {ECO:0000269|PubMed:19936047}.
CC -!- DISRUPTION PHENOTYPE: CoA-dependent KG oxidoreductase activity is
CC absent in a mutant strain deleted for both genes korA and korB, and
CC this strain is impaired for aerobic growth in the absence of sufficient
CC amounts of CO(2). Inhibition of the glyoxylate shunt or exclusion of
CC exogenous fatty acids alleviates this growth defect. Simultaneous
CC disruption of korAB and kgd results in strict dependence upon the
CC glyoxylate shunt for growth. {ECO:0000269|PubMed:19936047}.
CC -!- MISCELLANEOUS: Is extremely stable under aerobic conditions.
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DR EMBL; AL123456; CCP45247.1; -; Genomic_DNA.
DR PIR; E70864; E70864.
DR RefSeq; NP_216970.1; NC_000962.3.
DR RefSeq; WP_003412624.1; NZ_NVQJ01000024.1.
DR AlphaFoldDB; O53181; -.
DR SMR; O53181; -.
DR STRING; 83332.Rv2454c; -.
DR PaxDb; O53181; -.
DR PRIDE; O53181; -.
DR DNASU; 887435; -.
DR GeneID; 45426444; -.
DR GeneID; 887435; -.
DR KEGG; mtu:Rv2454c; -.
DR PATRIC; fig|83332.111.peg.2747; -.
DR TubercuList; Rv2454c; -.
DR eggNOG; COG1013; Bacteria.
DR InParanoid; O53181; -.
DR OMA; GNDTWTV; -.
DR PhylomeDB; O53181; -.
DR BioCyc; MetaCyc:G185E-6686-MON; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:MTBBASE.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 1: Evidence at protein level;
KW Magnesium; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..373
FT /note="2-oxoglutarate oxidoreductase subunit KorB"
FT /id="PRO_0000420517"
FT REGION 26..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 40143 MW; DBD5E9210DF33CC5 CRC64;
MTRSGDEAQL MTGVTGDLAG TELGLTPSLT KNAGVPTTDQ PQKGKDFTSD QEVRWCPGCG
DYVILNTIRN FLPELGLRRE NIVFISGIGC SSRFPYYLET YGFHSIHGRA PAIATGLALA
REDLSVWVVT GDGDALSIGG NHLIHALRRN INVTILLFNN RIYGLTKGQY SPTSEVGKVT
KSTPMGSLDH PFNPVSLALG AEATFVGRAL DSDRNGLTEV LRAAAQHRGA ALVEILQDCP
IFNDGSFDAL RKEGAEERVI KVRHGEPIVF GANGEYCVVK SGFGLEVAKT ADVAIDEIIV
HDAQVDDPAY AFALSRLSDQ NLDHTVLGIF RHISRPTYDD AARSQVVAAR NAAPSGTAAL
QSLLHGRDTW TVD
