KAMA_BACSU
ID KAMA_BACSU Reviewed; 471 AA.
AC O34676; O30469;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=L-lysine 2,3-aminomutase;
DE Short=LAM;
DE EC=5.4.3.2;
DE AltName: Full=KAM;
GN Name=kamA; OrderedLocusNames=BSU19690;
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=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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).
RN [3]
RP PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION, SUBUNIT, COFACTOR, AND MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 27505 / K49;
RX PubMed=10839984; DOI=10.1042/bj3480539;
RA Chen D., Ruzicka F.J., Frey P.A.;
RT "A novel lysine 2,3-aminomutase encoded by the yodO gene of bacillus
RT subtilis: characterization and the observation of organic radical
RT intermediates.";
RL Biochem. J. 348:539-549(2000).
RN [4]
RP MUTAGENESIS OF LYS-290; LYS-346 AND LYS-361.
RX PubMed=11148055; DOI=10.1021/bi002265w;
RA Chen D., Frey P.A.;
RT "Identification of lysine 346 as a functionally important residue for
RT pyridoxal 5'-phosphate binding and catalysis in lysine 2,3-aminomutase from
RT Bacillus subtilis.";
RL Biochemistry 40:596-602(2001).
RN [5]
RP FUNCTION, BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=21538109; DOI=10.1007/s00253-011-3301-8;
RA Muller S., Hoffmann T., Santos H., Saum S.H., Bremer E., Muller V.;
RT "Bacterial abl-like genes: production of the archaeal osmolyte N(epsilon)-
RT acetyl-beta-lysine by homologous overexpression of the yodP-kamA genes in
RT Bacillus subtilis.";
RL Appl. Microbiol. Biotechnol. 91:689-697(2011).
CC -!- FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta-
CC lysine. {ECO:0000269|PubMed:21538109}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine = (3S)-3,6-diaminohexanoate; Xref=Rhea:RHEA:19177,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:57434; EC=5.4.3.2;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10839984};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:10839984};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10839984};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.0 mM for L-lysine;
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10839984}.
CC -!- MASS SPECTROMETRY: Mass=54061; Mass_error=10; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10839984};
CC -!- DISRUPTION PHENOTYPE: Deletion of the genomic region encompassing the
CC entire yodT-yodS-yodR-yodQ-yodP-kamA gene cluster has no noticeable
CC effect on growth either in rich or minimal medium, does not affect
CC sporulation, and does not cause osmotic sensitivity or influence the
CC compatible solute pool of this soil bacterium.
CC {ECO:0000269|PubMed:21538109}.
CC -!- BIOTECHNOLOGY: The use of KamA and YodP from B.subtilis for N6-acetyl-
CC beta-lysine synthesis opens the bottleneck for the large-scale
CC production of N6-acetyl-beta-lysine to investigate its properties as a
CC compatible solute. {ECO:0000269|PubMed:21538109}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC {ECO:0000305}.
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DR EMBL; AF015775; AAB72069.1; -; Genomic_DNA.
DR EMBL; AF006665; AAB81159.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13860.1; -; Genomic_DNA.
DR PIR; B69904; B69904.
DR RefSeq; NP_389850.1; NC_000964.3.
DR RefSeq; WP_004399420.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34676; -.
DR SMR; O34676; -.
DR STRING; 224308.BSU19690; -.
DR PaxDb; O34676; -.
DR PRIDE; O34676; -.
DR EnsemblBacteria; CAB13860; CAB13860; BSU_19690.
DR GeneID; 940040; -.
DR KEGG; bsu:BSU19690; -.
DR PATRIC; fig|224308.179.peg.2156; -.
DR eggNOG; COG1509; Bacteria.
DR InParanoid; O34676; -.
DR OMA; PIWLNTH; -.
DR PhylomeDB; O34676; -.
DR BioCyc; BSUB:BSU19690-MON; -.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050066; F:lysine 2,3-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019475; P:L-lysine catabolic process to acetate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR025895; LAM_C_dom.
DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR InterPro; IPR022459; Lysine_aminomutase.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30538; PTHR30538; 1.
DR Pfam; PF12544; LAM_C; 1.
DR SFLD; SFLDF00283; L-lysine_2_3-aminomutase_(LAM; 1.
DR SFLD; SFLDG01070; PLP-dependent; 1.
DR TIGRFAMs; TIGR03820; lys_2_3_AblA; 1.
DR TIGRFAMs; TIGR00238; TIGR00238; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Isomerase;
KW Metal-binding; Pyridoxal phosphate; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..471
FT /note="L-lysine 2,3-aminomutase"
FT /id="PRO_0000172286"
FT DOMAIN 120..332
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT MOD_RES 346
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 290
FT /note="K->Q: More than 95% loss of activity, and half of
FT normal PLP binding capacity."
FT /evidence="ECO:0000269|PubMed:11148055"
FT MUTAGEN 346
FT /note="K->Q: No activity and no bound PLP."
FT /evidence="ECO:0000269|PubMed:11148055"
FT MUTAGEN 361
FT /note="K->Q: 95% loss of activity, normal PLP binding
FT capacity."
FT /evidence="ECO:0000269|PubMed:11148055"
FT CONFLICT 114
FT /note="P -> R (in Ref. 1; AAB81159)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="K -> R (in Ref. 1; AAB81159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 54074 MW; 7A9DA517BCA82FEC CRC64;
MKNKWYKPKR HWKEIELWKD VPEEKWNDWL WQLTHTVRTL DDLKKVINLT EDEEEGVRIS
TKTIPLNITP YYASLMDPDN PRCPVRMQSV PLSEEMHKTK YDLEDPLHED EDSPVPGLTH
RYPDRVLFLV TNQCSMYCRY CTRRRFSGQI GMGVPKKQLD AAIAYIRETP EIRDCLISGG
DGLLINDQIL EYILKELRSI PHLEVIRIGT RAPVVFPQRI TDHLCEILKK YHPVWLNTHF
NTSIEMTEES VEACEKLVNA GVPVGNQAVV LAGINDSVPI MKKLMHDLVK IRVRPYYIYQ
CDLSEGIGHF RAPVSKGLEI IEGLRGHTSG YAVPTFVVDA PGGGGKIALQ PNYVLSQSPD
KVILRNFEGV ITSYPEPENY IPNQADAYFE SVFPETADKK EPIGLSAIFA DKEVSFTPEN
VDRIKRREAY IANPEHETLK DRREKRDQLK EKKFLAQQKK QKETECGGDS S
