ABLA_METMP
ID ABLA_METMP Reviewed; 433 AA.
AC Q6LYX4;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=L-lysine 2,3-aminomutase;
DE Short=LAM;
DE EC=5.4.3.2;
GN Name=ablA; Synonyms=kamA; OrderedLocusNames=MMP0861;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP IDENTIFICATION, FUNCTION, GENE NAME, AND DISRUPTION PHENOTYPE.
RC STRAIN=S2 / LL;
RX PubMed=14532061; DOI=10.1128/aem.69.10.6047-6055.2003;
RA Pfluger K., Baumann S., Gottschalk G., Lin W., Santos H., Muller V.;
RT "Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of
RT methanogenic archaea are salt induced and are essential for the
RT biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.";
RL Appl. Environ. Microbiol. 69:6047-6055(2003).
CC -!- FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta-
CC lysine. Is involved in the biosynthesis pathway of N6-acetyl-beta-
CC lysine, a compatible solute produced by methanogenic archaea that helps
CC cells to cope with salt stress. {ECO:0000269|PubMed:14532061}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- DISRUPTION PHENOTYPE: Cells lacking both ablA and ablB no longer
CC produce N6-acetyl-beta-lysine and are incapable of growth at high salt
CC concentrations. {ECO:0000269|PubMed:14532061}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC {ECO:0000305}.
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DR EMBL; BX950229; CAF30417.1; -; Genomic_DNA.
DR RefSeq; WP_011170805.1; NC_005791.1.
DR AlphaFoldDB; Q6LYX4; -.
DR SMR; Q6LYX4; -.
DR STRING; 267377.MMP0861; -.
DR EnsemblBacteria; CAF30417; CAF30417; MMP0861.
DR GeneID; 2762078; -.
DR KEGG; mmp:MMP0861; -.
DR PATRIC; fig|267377.15.peg.886; -.
DR eggNOG; arCOG03246; Archaea.
DR HOGENOM; CLU_032161_0_0_2; -.
DR OMA; PIWLNTH; -.
DR OrthoDB; 10974at2157; -.
DR BioCyc; MMAR267377:MMP_RS04480-MON; -.
DR BRENDA; 5.4.3.2; 3262.
DR Proteomes; UP000000590; 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 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 Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004911; DUF160; 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 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Isomerase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine; Zinc.
FT CHAIN 1..433
FT /note="L-lysine 2,3-aminomutase"
FT /id="PRO_0000423062"
FT DOMAIN 122..334
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 136
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 348
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 433 AA; 49186 MW; 301B0F6A71B53AAA CRC64;
MNELSDESIL KYTKKISENA TIDNWNDYKW QLSNSIKDVD TLENFLGITF DEKEKTEIQK
AIDVFPMSIT PYYASLIDIK NLGKDPIYKQ SVASSKELIL ENFEMEDPLS EDEDSPVIGI
THRYPDRVLF YINPNCAMYC RHCTRKRKVS EKSSNPSKEE IQKAIDYIKN NNKIRDVLLS
GGDPLLLSDE FLDWILSEIS SIKHVELIRI GSRVPVVLPQ RITDNLVNVL KKYHPIWINT
HYNHPVEITK ESKKALDKLS DSGIPLGNQT VLLAGVNDCP YVMRKLNQKL VSSRVRPYYL
YQCDLSKGIS HFRTSVSKGL EIIESLIGHT TGFAVPRYVV DAPGGGGKIP VMPNYVVSWG
SDRVILRNYE GIITSYVEPS DYGGCSKNCD TCDRMCIGDF EINQTGIEKL ITDVDNSISL
IPENNERVAR RDD
