ABLA_METMA
ID ABLA_METMA Reviewed; 419 AA.
AC Q8PYC9;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=L-lysine 2,3-aminomutase;
DE Short=LAM;
DE EC=5.4.3.2;
GN Name=ablA; OrderedLocusNames=MM_0934;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP IDENTIFICATION, FUNCTION, GENE NAME, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
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 (Probable).
CC {ECO:0000305|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 -!- INDUCTION: Transcription is induced at high salt concentrations. Forms
CC part of an operon with ablB. {ECO:0000269|PubMed:14532061}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC {ECO:0000305}.
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DR EMBL; AE008384; AAM30630.1; -; Genomic_DNA.
DR RefSeq; WP_011032884.1; NC_003901.1.
DR AlphaFoldDB; Q8PYC9; -.
DR SMR; Q8PYC9; -.
DR STRING; 192952.MM_0934; -.
DR PRIDE; Q8PYC9; -.
DR EnsemblBacteria; AAM30630; AAM30630; MM_0934.
DR GeneID; 24876534; -.
DR KEGG; mma:MM_0934; -.
DR PATRIC; fig|192952.21.peg.1101; -.
DR eggNOG; arCOG03246; Archaea.
DR HOGENOM; CLU_032161_0_0_2; -.
DR OMA; PIWLNTH; -.
DR BRENDA; 5.4.3.2; 3270.
DR Proteomes; UP000000595; 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 PIRSF; PIRSF004911; DUF160; 1.
DR SFLD; SFLDF00283; L-lysine_2_3-aminomutase_(LAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR TIGRFAMs; TIGR03820; lys_2_3_AblA; 1.
DR TIGRFAMs; TIGR00238; TIGR00238; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Isomerase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine; Zinc.
FT CHAIN 1..419
FT /note="L-lysine 2,3-aminomutase"
FT /id="PRO_0000423061"
FT DOMAIN 112..323
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 338
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 419 AA; 47796 MW; 82D6DD937CD84D23 CRC64;
MKSRIKDCFN ASEEEFSDWK WQYRNRITTV EELEKLILLS DTEKRDIKKA LEVFPMAISP
YYASLIDPDD PECPVRLQAV PQSAELQKSS WELEDPLCED QDSPSEESCI THRYPDRVLF
LISNRCGMYC RHCTRKRRVG NREHDYSEKA IREGIEYIRM HHEVRDVLLS GGDALLVSDE
RLDWLLGELF SIPHVEIVRL GTRAPVTLPQ RITPELCEIL GKYPSVWLNT HFNHPKEITP
EAKKAMNMLA CAGIPLGNQS VLLRRVNDCP VIIKNLCHEL LKIKTRPYYL YQCDLSFGLE
HFRTSVARGI EIIEMLRGHT SGLAVPTFVV DAPGGGGKIP VGPNYLISSS DTGVTLRNYE
GVICVYPEPA EYSSKCQQKC TICDKHPGLK SDTGLARLYD EENDVIALEP EGLERKQRF
