KAMA_ACESD
ID KAMA_ACESD Reviewed; 414 AA.
AC E3PRJ8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=L-lysine 2,3-aminomutase {ECO:0000312|EMBL:CBH21502.1};
DE Short=LAM {ECO:0000250|UniProtKB:Q9XBQ8};
DE EC=5.4.3.2 {ECO:0000250|UniProtKB:Q9XBQ8};
DE AltName: Full=KAM {ECO:0000250|UniProtKB:Q9XBQ8};
GN Name=kamA; OrderedLocusNames=CLOST_1382;
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000269|PubMed:20937090};
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
CC -!- FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta-
CC lysine. {ECO:0000250|UniProtKB:Q9XBQ8}.
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 Evidence={ECO:0000250|UniProtKB:Q9XBQ8};
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|UniProtKB:Q9XBQ8};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9XBQ8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9XBQ8};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway. {ECO:0000250|UniProtKB:Q9XBQ8}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O34676}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP565809; CBH21502.1; -; Genomic_DNA.
DR AlphaFoldDB; E3PRJ8; -.
DR SMR; E3PRJ8; -.
DR STRING; 1511.CLOST_1382; -.
DR PRIDE; E3PRJ8; -.
DR EnsemblBacteria; CBH21502; CBH21502; CLOST_1382.
DR KEGG; cst:CLOST_1382; -.
DR eggNOG; COG1509; Bacteria.
DR HOGENOM; CLU_032161_0_0_9; -.
DR OMA; PIWLNTH; -.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000007041; 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 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..414
FT /note="L-lysine 2,3-aminomutase"
FT /id="PRO_0000416973"
FT DOMAIN 110..321
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
FT MOD_RES 336
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
SQ SEQUENCE 414 AA; 46991 MW; C8DF416B96229774 CRC64;
MSLKDKFFSH VSQEDWNDWK WQVRNRIETV EELKKYIPLT PEEEEGVKRC LDTLRMAITP
YYLSLIDVEN PNDPVRKQAV PLSLELHRAA SDQEDPLHED GDSPVPGLTH RYPDRVLLLM
TDQCSMYCRH CTRRRFAGQT DSAVDTKQID AAIEYIKNTP QVRDVLLSGG DALLISDEKL
EYTIKRLREI PHVEVIRIGS RVPVVMPQRI TPELVSMLKK YHPVWLNTHF NHPNEITEES
KRACELLADA GIPLGNQSVL LAGVNDCMHV MKKLVNDLVK IRVRPYYIYQ CDLSVGIEHF
RTPVAKGIEI IEGLRGHTSG YCVPTFVVDA PGGGGKTPVM PNYVISQNHN KVILRNFEGV
ITTYDEPDHY TFHCDCDVCT GKTNVHKVGV AGLLNGETAT LEPEGLERKQ RGHH
