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ID B4SIE5_STRM5 Unreviewed; 355 AA.
AC B4SIE5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 08-MAY-2019, entry version 84.
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=Smal_0445 {ECO:0000313|EMBL:ACF50150.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas;
OC Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50150.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF50150.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF50150.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC 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 ECO:0000256|SAAS:SAAS01117603};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC ECO:0000256|PIRSR:PIRSR600821-50,
CC ECO:0000256|SAAS:SAAS00373528};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00535998}.
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DR EMBL; CP001111; ACF50150.1; -; Genomic_DNA.
DR RefSeq; WP_004140567.1; NC_011071.1.
DR STRING; 391008.Smal_0445; -.
DR EnsemblBacteria; ACF50150; ACF50150; Smal_0445.
DR KEGG; smt:Smal_0445; -.
DR eggNOG; ENOG4105CJ4; Bacteria.
DR eggNOG; COG0787; LUCA.
DR HOGENOM; HOG000031446; -.
DR KO; K01775; -.
DR OMA; WEILCGF; -.
DR OrthoDB; 859043at2; -.
DR BioCyc; SMAL391008:SMAL_RS02290-MONOMER; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001867; 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 Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 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 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; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR00492; alr; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
DR PRODOM; B4SIE5.
DR SWISS-2DPAGE; B4SIE5.
KW Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW ECO:0000256|SAAS:SAAS00212336, ECO:0000313|EMBL:ACF50150.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00272807}.
FT DOMAIN 232 355 Ala_racemase_C. {ECO:0000259|SMART:
FT SM01005}.
FT ACT_SITE 33 33 Proton acceptor; specific for D-alanine.
FT {ECO:0000256|HAMAP-Rule:MF_01201}.
FT ACT_SITE 253 253 Proton acceptor; specific for L-alanine.
FT {ECO:0000256|HAMAP-Rule:MF_01201}.
FT BINDING 129 129 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT 52}.
FT BINDING 301 301 Substrate; via amide nitrogen.
FT {ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52}.
FT MOD_RES 33 33 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50}.
SQ SEQUENCE 355 AA; 38089 MW; 4E2A8253631DF59C CRC64;
MRPARALIDL GALRSNYRLA RELGGGKALA IIKADAYGHG AVRCAQALEG EADGFGVATI
EEALELRQAG IGAPILLLEG IFEASDMALV AEHDFWFAVG SPWQLEALAA FDSPRPLTVW
LKLDSGMHRL GLDVDSFRAA HARLSALPQV ERVVLMTHLA RADELDSERT HEQAATFARA
IDGLEGETSV CNSPALLGWP DVRSDWVRPG LMLYGANPLP DNTDLTARLR PVMTMQSKVI
AERWIESGEP VGYGARFVSK ARTRVGVVAL GYADGYPQFA PNGTPVLIDG QPGALIGRVS
MDMLTVDLTA HPQAGVGSVV ELWGNAPTLS ELAPRCGVSA YQLPCGVKRV ARVYM
//
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