ALR2_BACSU
ID ALR2_BACSU Reviewed; 394 AA.
AC P94494;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Alanine racemase 2 {ECO:0000255|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr2; Synonyms=yncD; OrderedLocusNames=BSU17640;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.;
RT "Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of
RT spoVJ.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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; U66480; AAB41097.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13648.1; -; Genomic_DNA.
DR PIR; F69888; F69888.
DR RefSeq; NP_389646.1; NC_000964.3.
DR RefSeq; WP_003244881.1; NZ_JNCM01000035.1.
DR PDB; 5IRP; X-ray; 2.10 A; A/B=1-394.
DR PDB; 6Q70; X-ray; 2.05 A; A/B=1-394.
DR PDB; 6Q71; X-ray; 1.92 A; A/B=1-394.
DR PDB; 6Q72; X-ray; 3.00 A; A/B/D/E=1-394.
DR PDBsum; 5IRP; -.
DR PDBsum; 6Q70; -.
DR PDBsum; 6Q71; -.
DR PDBsum; 6Q72; -.
DR AlphaFoldDB; P94494; -.
DR SMR; P94494; -.
DR STRING; 224308.BSU17640; -.
DR PaxDb; P94494; -.
DR PRIDE; P94494; -.
DR EnsemblBacteria; CAB13648; CAB13648; BSU_17640.
DR GeneID; 939550; -.
DR KEGG; bsu:BSU17640; -.
DR PATRIC; fig|224308.179.peg.1915; -.
DR eggNOG; COG0787; Bacteria.
DR InParanoid; P94494; -.
DR OMA; HMTHFSD; -.
DR PhylomeDB; P94494; -.
DR BioCyc; BSUB:BSU17640-MON; -.
DR BRENDA; 5.1.1.1; 658.
DR SABIO-RK; P94494; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001570; 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 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..394
FT /note="Alanine racemase 2"
FT /id="PRO_0000114501"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 272
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 179..197
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6Q71"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 338..345
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:6Q71"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:6Q71"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:6Q71"
SQ SEQUENCE 394 AA; 43648 MW; FE446C21107FBA6E CRC64;
MIKLCREVWI EVNLDAVKKN LRAIRRHIPH KSKIMAVVKA NGYGHGSIEV ARHALEHGAS
ELAVASVEEG IVLRKAGITA PILVLGFTSL SCVKKSAAWN ITLSAFQVDW MKEANEILEK
EASANRLAIH INVDTGMGRL GVRTKEELLE VVKALKASKF LRWTGIFTHF STADEPDTTL
TKLQHEKFIS FLSFLKKQGI ELPTVHMCNT AAAIAFPEFS ADMIRLGIGL YGLYPSAYIK
QLNLVKLEPA LSLKARIAYV KTMRTEPRTV SYGATYIAEP NEVIATLPIG YADGYSRALS
NRGFVLHRGK RVPVAGRVTM DMIMVSLGEN GEGKQGDEVV IYGKQKGAEI SVDEVAEMLN
TINYEVVSTL SRRIPRFYIR DGEIFKVSTP VLYV
