ALR_AERHH
ID ALR_AERHH Reviewed; 357 AA.
AC A0KH11;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000303|PubMed:24419381};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr-1 {ECO:0000312|EMBL:ABK36160.1};
GN OrderedLocusNames=AHA_1015 {ECO:0000312|EMBL:ABK36160.1};
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:4BHY}
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS), AND FUNCTION.
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: Catalyzes the interconversion of L-alanine and D-alanine.
CC Likely plays an important role in supplying D-alanine, which is an
CC indispensable constituent in the biosynthesis of bacterial cell-wall
CC peptidoglycan. {ECO:0000305|PubMed:24419381}.
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:0000255|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; CP000462; ABK36160.1; -; Genomic_DNA.
DR RefSeq; WP_011704949.1; NC_008570.1.
DR RefSeq; YP_855561.1; NC_008570.1.
DR PDB; 4BHY; X-ray; 3.25 A; A/B/C/D=1-357.
DR PDBsum; 4BHY; -.
DR AlphaFoldDB; A0KH11; -.
DR SMR; A0KH11; -.
DR STRING; 380703.AHA_1015; -.
DR EnsemblBacteria; ABK36160; ABK36160; AHA_1015.
DR KEGG; aha:AHA_1015; -.
DR PATRIC; fig|380703.7.peg.1019; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_0_6; -.
DR OMA; WEILCGF; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000000756; 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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..357
FT /note="Alanine racemase"
FT /id="PRO_0000446937"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 254
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:4BHY"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4BHY"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:4BHY"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:4BHY"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4BHY"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:4BHY"
SQ SEQUENCE 357 AA; 38774 MW; 8C552F85D7AF5CD9 CRC64;
MKAAIAQINT AALRHNLAVV KRHAPQCKII AVVKANAYGH GLLPVARTLV DADAYAVARI
EEALMLRSCA VVKPIVLLEG FFSAADLPVL AANNLQTAVH TWEQLEALEQ ADLPAPVVAW
LKLDTGMHRL GVRADEMPAF IERLAKCKNV VQPFNIMTHF SRSDELEQPT TREQIDLFSQ
LTAPLLGERA MANSAGILAW PDSHCDWVRP GVILYGVSPF PNTVAADYDL QPVMTLKTQL
IAVRDHKAGE PVGYGANWVS DRDTRLGVIA IGYGDGYPRM APNGTPVLVN GRIVPLVGRV
SMDMTTVDLG PGATDKAGDE AVLWGEGLPV ERVADQIGTI PYELITKLTS RVFMEYV
