ID   ARAA_BACSU              Reviewed;         496 AA.
AC   P94523; O05184;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=L-arabinose isomerase {ECO:0000255|HAMAP-Rule:MF_00519};
DE            EC=5.3.1.4 {ECO:0000255|HAMAP-Rule:MF_00519};
GN   Name=araA {ECO:0000255|HAMAP-Rule:MF_00519}; OrderedLocusNames=BSU28800;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9084180; DOI=10.1099/00221287-143-3-957;
RA   Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H.;
RT   "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence,
RT   genetic organization and expression.";
RL   Microbiology 143:957-969(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
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).
RN   [4]
RP   SEQUENCE REVISION TO 85-94.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   TRANSCRIPTIONAL REGULATION.
RX   PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x;
RA   Mota L.J., Tavares P., Sa-Nogueira I.M.G.;
RT   "Mode of action of AraR, the key regulator of L-arabinose metabolism in
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 33:476-489(1999).
CC   -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose.
CC       {ECO:0000255|HAMAP-Rule:MF_00519}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-L-arabinopyranose = L-ribulose; Xref=Rhea:RHEA:14821,
CC         ChEBI:CHEBI:16880, ChEBI:CHEBI:40886; EC=5.3.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00519};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00519};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC       step 1/3. {ECO:0000255|HAMAP-Rule:MF_00519}.
CC   -!- INDUCTION: Transcription is repressed by glucose and by the binding of
CC       AraR to the operon promoter. L-arabinose acts as an inducer by
CC       inhibiting the binding of AraR to the DNA, thus allowing expression of
CC       the gene. {ECO:0000269|PubMed:10417639}.
CC   -!- SIMILARITY: Belongs to the arabinose isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00519}.
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DR   EMBL; X89408; CAA61585.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99587.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14840.2; -; Genomic_DNA.
DR   PIR; C69587; C69587.
DR   RefSeq; NP_390758.2; NC_000964.3.
DR   RefSeq; WP_003229499.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P94523; -.
DR   SMR; P94523; -.
DR   STRING; 224308.BSU28800; -.
DR   jPOST; P94523; -.
DR   PRIDE; P94523; -.
DR   EnsemblBacteria; CAB14840; CAB14840; BSU_28800.
DR   GeneID; 936764; -.
DR   KEGG; bsu:BSU28800; -.
DR   PATRIC; fig|224308.179.peg.3128; -.
DR   eggNOG; COG2160; Bacteria.
DR   InParanoid; P94523; -.
DR   OMA; HMLEICP; -.
DR   PhylomeDB; P94523; -.
DR   BioCyc; BSUB:BSU28800-MON; -.
DR   BRENDA; 5.3.1.4; 658.
DR   UniPathway; UPA00145; UER00565.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008733; F:L-arabinose isomerase activity; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IBA:GO_Central.
DR   Gene3D; 3.40.50.10940; -; 1.
DR   HAMAP; MF_00519; Arabinose_Isome; 1.
DR   InterPro; IPR024664; Ara_Isoase_C.
DR   InterPro; IPR038583; AraA_N_sf.
DR   InterPro; IPR004216; Fuc/Ara_isomerase_C.
DR   InterPro; IPR009015; Fucose_isomerase_N/cen_sf.
DR   InterPro; IPR003762; Lara_isomerase.
DR   PANTHER; PTHR38464; PTHR38464; 1.
DR   Pfam; PF11762; Arabinose_Iso_C; 1.
DR   Pfam; PF02610; Arabinose_Isome; 1.
DR   PIRSF; PIRSF001478; L-ara_isomerase; 1.
DR   SUPFAM; SSF50443; SSF50443; 1.
DR   SUPFAM; SSF53743; SSF53743; 1.
PE   2: Evidence at transcript level;
KW   Arabinose catabolism; Carbohydrate metabolism; Isomerase; Manganese;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..496
FT                   /note="L-arabinose isomerase"
FT                   /id="PRO_0000198382"
FT   BINDING         305
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         330
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   BINDING         446
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00519"
FT   CONFLICT        85..94
FT                   /note="AKMWIEGLSS -> SQKLWKRRPFPP (in Ref. 2; CAA99587)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  56122 MW;  E0DCF8B736364F18 CRC64;
     MLQTKDYEFW FVTGSQHLYG EETLELVDQH AKSICEGLSG ISSRYKITHK PVVTSPETIR
     ELLREAEYSE TCAGIITWMH TFSPAKMWIE GLSSYQKPLM HLHTQYNRDI PWGTIDMDFM
     NSNQSAHGDR EYGYINSRMG LSRKVIAGYW DDEEVKKEMS QWMDTAAALN ESRHIKVARF
     GDNMRHVAVT DGDKVGAHIQ FGWQVDGYGI GDLVEVMDRI TDDEVDTLYA EYDRLYVISE
     ETKRDEAKVA SIKEQAKIEL GLTAFLEQGG YTAFTTSFEV LHGMKQLPGL AVQRLMEKGY
     GFAGEGDWKT AALVRMMKIM AKGKRTSFME DYTYHFEPGN EMILGSHMLE VCPTVALDQP
     KIEVHSLSIG GKEDPARLVF NGISGSAIQA SIVDIGGRFR LVLNEVNGQE IEKDMPNLPV
     ARVLWKPEPS LKTAAEAWIL AGGAHHTCLS YELTAEQMLD WAEMAGIESV LISRDTTIHK
     LKHELKWNEA LYRLQK