ID I3VUF8_THESW Unreviewed; 388 AA.
AC I3VUF8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN OrderedLocusNames=Tsac_1140 {ECO:0000313|EMBL:AFK86153.1};
OS Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86153.1, ECO:0000313|Proteomes:UP000006178};
RN [1] {ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA Brown S.D., Land M.L., Herring C.D.;
RT "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFK86153.1, ECO:0000313|Proteomes:UP000006178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT Thermoanaerobacterium saccharolyticum during the Degradation of
RT Hemicellulose.";
RL Appl. Environ. Microbiol. 80:5001-5011(2014).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; CP003184; AFK86153.1; -; Genomic_DNA.
DR RefSeq; WP_014758037.1; NC_017992.1.
DR AlphaFoldDB; I3VUF8; -.
DR STRING; 1094508.Tsac_1140; -.
DR KEGG; tsh:Tsac_1140; -.
DR PATRIC; fig|1094508.3.peg.1153; -.
DR eggNOG; COG0787; Bacteria.
DR BioCyc; TSAC1094508:GLMA-1162-MONOMER; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000006178; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 246..374
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 267
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 388 AA; 43759 MW; A0E392C6556AAD01 CRC64;
MFNLYRPTWA EVNLDNIIHN YKEIRKITDK NAGIMAVVKA NAYGHGSYEV SKELINCGVD
YLAVATIDEA LELREQGISK PILVLGYTPA KFADVFIKYD ITQTAFELSY VKEVAKVAQK
LGKDAKIHVK IDTGMGRIGY NDMNKAYEEI LSMSSLSGIN IEGIFSHFSS SDEKDKEYTV
RQLKIFLSLI ERLKKSGIYI PIRHIANSAA ILDMPETHLD MVRPGIILYG SFPSDEVNKK
IDLRPTISLR SKVVYVKDVE KGEYISYNRT YRTNRKSRIA TLPIGYADGL NRLLSNNHNV
IINGKYAPIV GKICMDQCMI DVTPIEDVKE GDTATIMGEA DGKFISADEI AKKLKTISYE
VYCGISRRVP RIYIFNGEIT KVENYLKC
//
