BSR_AERHH
ID BSR_AERHH Reviewed; 408 AA.
AC A0KLG5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Broad specificity amino-acid racemase {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305|PubMed:24419381};
DE EC=5.1.1.10 {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:24419381};
DE AltName: Full=Broad spectrum racemase {ECO:0000303|PubMed:24419381};
DE Flags: Precursor;
GN Name=bsr {ECO:0000303|PubMed:24419381};
GN Synonyms=alr-3 {ECO:0000312|EMBL:ABK37415.1};
GN OrderedLocusNames=AHA_2607 {ECO:0000312|EMBL:ABK37415.1};
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC 2358 / NCIMB 9240 / NCTC 8049;
RX PubMed=16980456; DOI=10.1128/jb.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
RN [2] {ECO:0007744|PDB:4BF5}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, DISULFIDE
RP BOND, AND PYRIDOXAL PHOSPHATE AT LYS-74.
RX PubMed=24419381; DOI=10.1107/s1399004713024838;
RA Espaillat A., Carrasco-Lopez C., Bernardo-Garcia N., Pietrosemoli N.,
RA Otero L.H., Alvarez L., de Pedro M.A., Pazos F., Davis B.M., Waldor M.K.,
RA Hermoso J.A., Cava F.;
RT "Structural basis for the broad specificity of a new family of amino-acid
RT racemases.";
RL Acta Crystallogr. D 70:79-90(2014).
CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC substrates. Reversibly racemizes ten of the 19 natural chiral amino
CC acids known, including both non-beta-branched aliphatic amino acids
CC (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino
CC acids (His, Lys and Arg). Is not active on negatively charged (Glu and
CC Asp) or aromatic (Tyr, Trp and Phe) amino acids and displays minimal
CC activity towards beta-branched aliphatic (Ile, Val and Thr) substrates
CC (PubMed:24419381). Enables bacteria to produce and release
CC extracellular non-canonical D-amino acids (NCDAAs) that regulate
CC diverse cellular processes (By similarity).
CC {ECO:0000250|UniProtKB:Q9KSE5, ECO:0000269|PubMed:24419381}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:32557; Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02212, ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine = D-methionine; Xref=Rhea:RHEA:12492,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57932;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucine = D-leucine; Xref=Rhea:RHEA:59396,
CC ChEBI:CHEBI:57427, ChEBI:CHEBI:143079;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine = D-cysteine; Xref=Rhea:RHEA:59272,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:35236;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine = D-glutamine; Xref=Rhea:RHEA:59276,
CC ChEBI:CHEBI:58000, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine = D-asparagine; Xref=Rhea:RHEA:59280,
CC ChEBI:CHEBI:58048, ChEBI:CHEBI:74337;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine = D-histidine; Xref=Rhea:RHEA:59188,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:142967;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:24419381};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:24419381}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q9KSE5,
CC ECO:0000255|HAMAP-Rule:MF_02212}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305}.
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DR EMBL; CP000462; ABK37415.1; -; Genomic_DNA.
DR RefSeq; WP_011706424.1; NC_008570.1.
DR RefSeq; YP_857116.1; NC_008570.1.
DR PDB; 4BF5; X-ray; 1.45 A; A/B=1-408.
DR PDBsum; 4BF5; -.
DR AlphaFoldDB; A0KLG5; -.
DR SMR; A0KLG5; -.
DR STRING; 380703.AHA_2607; -.
DR EnsemblBacteria; ABK37415; ABK37415; AHA_2607.
DR GeneID; 64359132; -.
DR KEGG; aha:AHA_2607; -.
DR PATRIC; fig|380703.7.peg.2608; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_6; -.
DR OMA; TSMNTVM; -.
DR Proteomes; UP000000756; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR GO; GO:0047679; F:arginine racemase activity; IEA:RHEA.
DR GO; GO:0018113; F:lysine racemase activity; IEA:RHEA.
DR GO; GO:0018111; F:methionine racemase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030378; F:serine racemase activity; IEA:RHEA.
DR CDD; cd06826; PLPDE_III_AR2; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_02212; Bsr_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 InterPro; IPR043698; Racemase_Bsr/Lyr.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Isomerase; Periplasm; Pyridoxal phosphate;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT CHAIN 22..408
FT /note="Broad specificity amino-acid racemase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT /id="PRO_5002625282"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT MOD_RES 74
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212,
FT ECO:0000269|PubMed:24419381, ECO:0007744|PDB:4BF5"
FT DISULFID 70..96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212,
FT ECO:0007744|PDB:4BF5"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 210..230
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:4BF5"
FT HELIX 392..401
FT /evidence="ECO:0007829|PDB:4BF5"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:4BF5"
SQ SEQUENCE 408 AA; 44575 MW; 007C554833DF53B1 CRC64;
MHKKTLLATL ILGLLAGQAV AAPYLPLASD HRNGEVQTAS NAWLEVDLGA FEHNIQTLKD
RLGDKGPKIC AIMKADAYGH GIDLLVPSVV KAGIPCIGIA SNEEARVARE KGFTGRLMRV
RAATPAEVEQ ALPYKMEELI GSLVSAQGIA DIAQRHHTNI PVHIALNSAG MSRNGIDLRL
ADSKEDALAM LKLKGITPVG IMTHFPVEEK EDVKMGLAQF KLDSQWLLEA GKLDRSKITI
HAANSFATLE VPDAYFDMVR PGGLLYGDSI PSYTEYKRVM AFKTQVASVN HYPAGNTVGY
DRTFTLKRDS WLANLPLGYS DGYRRALSNK AYVLIQGQKV PVVGKTSMNT IMVDVTDLKG
VKPGDEVVLF GRQGEAEVKQ ADLEEYNGAL LADMYTIWGY TNPKKIKR
