ID E4ME17_9BACT Unreviewed; 792 AA.
AC E4ME17;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
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:EFR56805.1};
GN ORFNames=HMPREF9720_1974 {ECO:0000313|EMBL:EFR56805.1};
OS Alistipes sp. HGB5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=908612 {ECO:0000313|EMBL:EFR56805.1, ECO:0000313|Proteomes:UP000002960};
RN [1] {ECO:0000313|EMBL:EFR56805.1, ECO:0000313|Proteomes:UP000002960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB5 {ECO:0000313|EMBL:EFR56805.1,
RC ECO:0000313|Proteomes:UP000002960};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-2010) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFR56805.1}.
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DR EMBL; AENZ01000069; EFR56805.1; -; Genomic_DNA.
DR RefSeq; WP_009598625.1; NZ_AENZ01000069.1.
DR AlphaFoldDB; E4ME17; -.
DR PATRIC; fig|908612.3.peg.2412; -.
DR eggNOG; COG0770; Bacteria.
DR eggNOG; COG0787; Bacteria.
DR OrthoDB; 9801978at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000002960; 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}.
FT DOMAIN 663..790
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 460
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 684
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 558
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 733
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 460
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 792 AA; 86837 MW; 1338873E76821A66 CRC64;
MNYRLSRIAA ICGGKFSGCD SEVRSVVTDS RSLSCELGCR PMFVAMRGAN HDSHDFIADM
QSRGVRAFLV ERGVEASSCT GECGFVQVDN AIEALQRLAA YHRAQFRGTV VGITGSNGKT
VIKEWIAEEL PEGMKYYRSP KSYNSQLGVP LSVLMLEGDE ELAIFEAGIS KPGEMERLER
IIRPDAVIFT SIGDAHQENF INLEQKCDEK MILARSASKI IYHSYYEPLG RMVAAHFADR
RPVDAASYPE VPESVIGNAA SRRNAQIVEA FCDAMRYPAP SFAGAPSVAM RLEVKEGIND
SILINDAYNL DLNSLALALD YLHSVALSRR RTLVLSDISQ SGLSDDELYG RVAGMVARAG
IDFLIGIGPR LKRYAALFAC DKEFFTATDE CVARINRDAV AGRAILLKGA RDFRFEKLVH
LLSRKSHTTV LEVDLDAMIH NLNYFRSKLS FGTRLVAMVK AGSYGAGDFE VAQMLQHQGV
DYLAVAFADE GVLLRERGIS MPIVVLNADA DSFDVMIANR LEPEIYSFHS LGAFADAVTH
AGESRYPIHV KLDTGMHRLG FVEQEIAQLC ATLAATPQVK AASVFSHLNC ADMPEEDAYT
RAQIALYDRM SAQLAASLPY PVIRHTANSA AIERFPEAQF DMCRLGLGLY GFGFRHNDAL
RPVSTLKTRI VQIKRLPAGD AVGYGRAGKL TRPTTTATIP IGYADGLDRH LGCGRWSVLV
AGQPAPIIGR VCMDSCMIDI TDIPGVKEGD EVSVFSPVPG NDLETMARVL DTISYEIMTS
VSGRVKRIYL KE
//
