ID V2Q9A2_9BACT Unreviewed; 377 AA.
AC V2Q9A2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:USF23203.1};
GN ORFNames=N508_000259 {ECO:0000313|EMBL:USF23203.1}, N508_01444
GN {ECO:0000313|EMBL:ESJ97521.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ97521.1};
RN [1] {ECO:0000313|EMBL:ESJ97521.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ97521.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF23203.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23203.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF23203.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23203.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYGZ01000018; ESJ97521.1; -; Genomic_DNA.
DR EMBL; CP097562; USF23203.1; -; Genomic_DNA.
DR RefSeq; WP_023276271.1; NZ_FTRD01000001.1.
DR AlphaFoldDB; V2Q9A2; -.
DR STRING; 1379858.N508_01444; -.
DR GeneID; 78586999; -.
DR PATRIC; fig|1379858.3.peg.1445; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_0; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000017429; 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}; Reference proteome {ECO:0000313|Proteomes:UP000017429}.
FT DOMAIN 244..368
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 45
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 265
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 45
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 377 AA; 42500 MW; 94F2CCF7E1D89BCF CRC64;
MKINSLDNMG IIPRPTYAVI DMKRFGSNID IARNLSKSDI IAVVKADAYG HGAKVLAKYA
YEEKNIRNFA VATMIEGIEL RKVLSSKDTK IVVLGYVSDS FVKEALQASL TLPVFDYRYA
EIISKAAKEL DIEAHVALEI DTGMSRLGFS YEIQLLELLK QYKNIHVDFA ISHLATSDCD
NSYAHIQTER FDKFLEINKG YTFATSFLNS SGIANFENRW TFTRPGLFLY GYESTNVIKD
LQPVMSLWSE IAHVKFLKKG ESVGYGRTFF APKDMIIGVI PIGYADGYRR SFSNKGYVLA
GNIKCHVIGN VCMDMTMIDV TELGKNCIGQ KVQIMGDDIT ASTLSRWADT IEYEILCGIS
DRVPRVYKYE EGYFEIF
//
