ID A0A379MQU7_9BACT Unreviewed; 797 AA.
AC A0A379MQU7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN Name=alr {ECO:0000313|EMBL:SUE33893.1};
GN ORFNames=NCTC11190_01107 {ECO:0000313|EMBL:SUE33893.1};
OS Rikenella microfusus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Rikenella.
OX NCBI_TaxID=28139 {ECO:0000313|EMBL:SUE33893.1, ECO:0000313|Proteomes:UP000255233};
RN [1] {ECO:0000313|EMBL:SUE33893.1, ECO:0000313|Proteomes:UP000255233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11190 {ECO:0000313|EMBL:SUE33893.1,
RC ECO:0000313|Proteomes:UP000255233};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; UGVL01000001; SUE33893.1; -; Genomic_DNA.
DR RefSeq; WP_027290227.1; NZ_UGVL01000001.1.
DR AlphaFoldDB; A0A379MQU7; -.
DR STRING; 880526.GCA_000427365_00340; -.
DR GeneID; 78538302; -.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000255233; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 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; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR035911; MurE/MurF_N.
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 Pfam; PF08245; Mur_ligase_M; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 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}; Reference proteome {ECO:0000313|Proteomes:UP000255233}.
FT DOMAIN 670..795
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 469
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 691
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 567
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 740
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 469
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 797 AA; 86854 MW; 9138DC10E8AA1D15 CRC64;
MDYTLSHIAA VTGGALHGDD RRVAAVATDS RNSIAAPGET LFVALVGPNH DGHRYIEELY
RRGVRSFLVG YVPDPPAAPM PDASFVTVPD TLDALQALAA YHRQQYNGTV AAITGSNGKT
VVKEWIAQLW PEGAGRLFRS PRSYNSQLGV ALSLLMIRGD EQLVVIEAGI SRPGEMERLE
AMIRPQIGIL TNIGAAHGEN FNSDEQKLDE KLKLFRNAES IIYRADIPLI AKHIGKRYGK
CPERLHGWRT DLATGLAEHF GDYASRENAA HVVALYRLLG IAPKPLDGLQ PVAMRLELRE
GILGSTVIND SYNSDLTSLG IALDYLDHNA GDRPKALILS DILQAGLKSD ELYRQVAALV
REHGIADFTG IGPGIASAAH HFVALLGSEH VHLHAATDDF LRHIDKERFA GRFILVKGSR
AFGFERISRM LEKRTHTTTL EVNLGALAAN LGHFRAMLRP GTRVMAMVKA HSYGTGSVEI
AAMLQHEGVD YLAVAFADEG VALREAGIRL PIVVLNSDPG SFAVMADYDL EPEIYSFSSL
KGYAAEIRSR GITEAPIHLK MDTGMHRLGF MPQELPELCV LLKDEHAVKV RSIFSHLAAS
EDPAEDDFTR GQIALFTRMS GRIVETLGDP SILRHICNSA GIARFPEAHF DMVRLGVGLY
GIEDPALQAA ATLRTQIVQI KTLDRGDTVG YNRRGVATGP MRTATIPIGY ADGMDRGLGR
GAGQVCIRGV LCPTFGNICM DTCMIDITAV PEAREGDEVV IFGERPTVRE VAEVLGTISY
EVLTSVSARI KRIYVRE
//
