LARA_THETC
ID LARA_THETC Reviewed; 426 AA.
AC D9TQ02;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Lactate racemase {ECO:0000303|PubMed:24710389};
DE Short=Lar {ECO:0000303|PubMed:24710389};
DE EC=5.1.2.1 {ECO:0000269|PubMed:24710389};
GN Name=larA {ECO:0000303|PubMed:24710389};
GN OrderedLocusNames=Tthe_1662 {ECO:0000312|EMBL:ADL69171.1};
OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS thermosaccharolyticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX NCBI_TaxID=580327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC 00135 / 2032;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT 571.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=24710389; DOI=10.1038/ncomms4615;
RA Desguin B., Goffin P., Viaene E., Kleerebezem M., Martin-Diaconescu V.,
RA Maroney M.J., Declercq J.P., Soumillion P., Hols P.;
RT "Lactate racemase is a nickel-dependent enzyme activated by a widespread
RT maturation system.";
RL Nat. Commun. 5:3615-3615(2014).
CC -!- FUNCTION: Catalyzes the interconversion between the D- and L-isomers of
CC lactate. {ECO:0000269|PubMed:24710389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate = (R)-lactate; Xref=Rhea:RHEA:10960,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:16651; EC=5.1.2.1;
CC Evidence={ECO:0000269|PubMed:24710389};
CC -!- COFACTOR:
CC Name=Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide;
CC Xref=ChEBI:CHEBI:137373; Evidence={ECO:0000250|UniProtKB:F9USS9};
CC Note=Was originally shown to use Ni(2+) as a cofactor
CC (PubMed:24710389), but in fact, the cofactor is a (SCS)Ni complex, a
CC nicotinic acid mononucleotide derivative that is covalently attached to
CC Lys-184 and forms a tridentate pincer complex that coordinates nickel
CC through one metal-carbon and two metal-sulfur bonds (By similarity).
CC {ECO:0000250|UniProtKB:F9USS9, ECO:0000269|PubMed:24710389};
CC -!- ACTIVITY REGULATION: Activation of the apo-enzyme requires the three
CC accessory proteins LarB, LarE and LarC, that are involved in the
CC biosynthesis of the nickel-pincer cofactor of LarA.
CC {ECO:0000250|UniProtKB:F9USS9, ECO:0000305|PubMed:24710389}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 mM for L-lactate {ECO:0000269|PubMed:24710389};
CC KM=3 mM for D-lactate {ECO:0000269|PubMed:24710389};
CC Note=kcat is 986 sec(-1) for conversion of L-lactate to D-lactate.
CC kcat is 551 sec(-1) for conversion of D-lactate to L-lactate.
CC {ECO:0000269|PubMed:24710389};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:24710389}.
CC -!- SIMILARITY: Belongs to the lactate racemase family. {ECO:0000305}.
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DR EMBL; CP002171; ADL69171.1; -; Genomic_DNA.
DR RefSeq; WP_013298138.1; NC_014410.1.
DR PDB; 2YJG; X-ray; 1.80 A; A/B=1-426.
DR PDBsum; 2YJG; -.
DR AlphaFoldDB; D9TQ02; -.
DR SMR; D9TQ02; -.
DR STRING; 580327.Tthe_1662; -.
DR EnsemblBacteria; ADL69171; ADL69171; Tthe_1662.
DR KEGG; ttm:Tthe_1662; -.
DR eggNOG; COG3875; Bacteria.
DR HOGENOM; CLU_050189_0_0_9; -.
DR OMA; HEEGCKF; -.
DR OrthoDB; 313921at2; -.
DR Proteomes; UP000001626; Chromosome.
DR GO; GO:0050043; F:lactate racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.226.30; -; 1.
DR InterPro; IPR043166; LarA-like_C.
DR InterPro; IPR018657; LarA-like_N.
DR Pfam; PF09861; Lar_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..426
FT /note="Lactate racemase"
FT /id="PRO_0000441652"
FT ACT_SITE 108
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:F9USS9"
FT ACT_SITE 174
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:F9USS9"
FT BINDING 72..75
FT /ligand="Ni(II)-pyridinium-3,5-bisthiocarboxylate
FT mononucleotide"
FT /ligand_id="ChEBI:CHEBI:137373"
FT /evidence="ECO:0000250|UniProtKB:F9USS9"
FT BINDING 184
FT /ligand="Ni(II)-pyridinium-3,5-bisthiocarboxylate
FT mononucleotide"
FT /ligand_id="ChEBI:CHEBI:137373"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:F9USS9"
FT BINDING 200
FT /ligand="Ni(II)-pyridinium-3,5-bisthiocarboxylate
FT mononucleotide"
FT /ligand_id="ChEBI:CHEBI:137373"
FT /ligand_part="Ni"
FT /ligand_part_id="ChEBI:CHEBI:28112"
FT /evidence="ECO:0000250|UniProtKB:F9USS9"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F9USS9"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:F9USS9"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2YJG"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2YJG"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2YJG"
FT TURN 186..190
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:2YJG"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 307..316
FT /evidence="ECO:0007829|PDB:2YJG"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 326..333
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 338..346
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:2YJG"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:2YJG"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:2YJG"
SQ SEQUENCE 426 AA; 46879 MW; FBC204F4B8CC0212 CRC64;
MANIEIPYGK SKLAFDLPDE RIQGILRSKA GSYKVNMSEE DIVKRALENP IGTKRLQDLA
EGKKNIVIIT SDHTRPVPSR ITLPLLLDEI RKKNKSANVK ILIATGFHRG TTLQEMKAKF
GEDLVENEQF VVHDSRNSEN MELIGTLPSG GKLEINKLAV EADLLVAEGF IEPHFFAGFS
GGRKSILPGI ASVQCILANH CSEFIKNPYA RTGVLENNPI HRDMIYAAKK ANLAFILNVV
IDSSHKIVNA FAGHSEKAHL KGCEFVSEIA TVNAKPADIV ITSNGGYPLD QNIYQSVKGM
TAGEAACKDG GVIIIAAECA DGHGGEGFYR WFKESKDPQD VMNKILSRGR DETLPDQWEA
QILARILINH KVIMVTDSKN YEYVKDMFMT PAKDLGEALK IAESIVNNDS KINVIPDGVS
VIVREK
