ID ALR_STRCO Reviewed; 391 AA.
AC O86786;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr; OrderedLocusNames=SCO4745; ORFNames=SC6G4.23;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000255|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: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; AL939121; CAA20401.1; -; Genomic_DNA.
DR PIR; T35574; T35574.
DR RefSeq; NP_628903.1; NC_003888.3.
DR RefSeq; WP_011029835.1; NZ_VNID01000016.1.
DR PDB; 5FAC; X-ray; 2.80 A; A/B/C/D=1-391.
DR PDB; 5FAG; X-ray; 1.51 A; A/B/C/D=1-391.
DR PDB; 5FAJ; X-ray; 1.64 A; A/B/C/D=1-391.
DR PDBsum; 5FAC; -.
DR PDBsum; 5FAG; -.
DR PDBsum; 5FAJ; -.
DR AlphaFoldDB; O86786; -.
DR SMR; O86786; -.
DR STRING; 100226.gene:17762394; -.
DR PaxDb; 100226-SCO4745; -.
DR PATRIC; fig|100226.15.peg.4817; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_0_0_11; -.
DR InParanoid; O86786; -.
DR OrthoDB; 9813814at2; -.
DR PhylomeDB; O86786; -.
DR BRENDA; 5.1.1.1; 5998.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..391
FT /note="Alanine racemase"
FT /id="PRO_0000114580"
FT ACT_SITE 46
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 283
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 46
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:5FAG"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5FAJ"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 191..209
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:5FAG"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:5FAJ"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:5FAG"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 362..368
FT /evidence="ECO:0007829|PDB:5FAG"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:5FAG"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:5FAG"
SQ SEQUENCE 391 AA; 41200 MW; 24754AC1385DCA1B CRC64;
MSETTARRDA DAVLRARAEI DLAALRANVR ALRERAPGAA LMAVVKADAY GHGAIPCARA
AVAAGATWLG TATPQEALAL RAAEPGLPDD VRIMCWLWTP GGPWREAVEA RLDVSVSAMW
AMEEVTGAAR AAGVPARVQL KADTGLGRGG CQPGADWERL VGAALRAEEE GLLRVTGLWS
HFACADEPGH PSIAAQLTRF REMTAYAEQR GLRPEVRHIA NSPATLTLPD AHFDLVRPGI
AMYGVSPSPE IGTPADFGLR PVMTLAASLA LVKQVPGGHG VSYGHHYTTP GETTLGLVPL
GYADGIPRHA SSSGPVLVDG KWRTVAGRIA MDQFVVDLGG DRPEPGAEAV LFGPGDRGEP
TAEDWAQAAG TIAYEIVTRI GSRVPRVYVN E
//
