KAMA_FUSNN
ID KAMA_FUSNN Reviewed; 425 AA.
AC Q8RHX4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=L-lysine 2,3-aminomutase {ECO:0000303|PubMed:6811551};
DE Short=LAM {ECO:0000250|UniProtKB:Q9XBQ8};
DE EC=5.4.3.2 {ECO:0000269|PubMed:6811551};
DE AltName: Full=KAM {ECO:0000303|PubMed:17166837};
GN Name=kamA {ECO:0000250|UniProtKB:Q9XBQ8}; OrderedLocusNames=FN1866;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:6811551};
RX PubMed=6811551; DOI=10.1128/jb.152.1.201-207.1982;
RA Barker H.A., Kahn J.M., Hedrick L.;
RT "Pathway of lysine degradation in Fusobacterium nucleatum.";
RL J. Bacteriol. 152:201-207(1982).
RN [3] {ECO:0000305}
RP IDENTIFICATION.
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355 {ECO:0000269|PubMed:17166837};
RX PubMed=17166837; DOI=10.1074/jbc.m609829200;
RA Kreimeyer A., Perret A., Lechaplais C., Vallenet D., Medigue C.,
RA Salanoubat M., Weissenbach J.;
RT "Identification of the last unknown genes in the fermentation pathway of
RT lysine.";
RL J. Biol. Chem. 282:7191-7197(2007).
CC -!- FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta-
CC lysine. {ECO:0000269|PubMed:6811551}.
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:0000269|PubMed:6811551};
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 -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway. {ECO:0000269|PubMed:6811551}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9XBQ8}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC {ECO:0000305}.
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DR EMBL; AE009951; AAL93965.1; -; Genomic_DNA.
DR RefSeq; NP_602666.1; NC_003454.1.
DR AlphaFoldDB; Q8RHX4; -.
DR SMR; Q8RHX4; -.
DR STRING; 190304.FN1866; -.
DR PRIDE; Q8RHX4; -.
DR EnsemblBacteria; AAL93965; AAL93965; FN1866.
DR KEGG; fnu:FN1866; -.
DR PATRIC; fig|190304.8.peg.342; -.
DR eggNOG; COG1509; Bacteria.
DR HOGENOM; CLU_032161_0_0_0; -.
DR InParanoid; Q8RHX4; -.
DR OMA; PIWLNTH; -.
DR BioCyc; FNUC190304:G1FZS-363-MON; -.
DR BioCyc; MetaCyc:MON-12292; -.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000002521; 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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Isomerase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..425
FT /note="L-lysine 2,3-aminomutase"
FT /id="PRO_0000416974"
FT DOMAIN 113..325
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 127
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 134
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 MOD_RES 339
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9XBQ8"
SQ SEQUENCE 425 AA; 48747 MW; AAF906FD30272D31 CRC64;
MNTVNTRKKF FPNVTDEEWN DWTWQVKNRL ESVEDLKKYV DLSEEETEGV VRTLETLRMA
ITPYYFSLID LNSDRCPIRK QAIPTIQEIH QSDADLLDPL HEDEDSPVPG LTHRYPDRVL
LLITDMCSMY CRHCTRRRFA GSSDDAMPMD RIDKAIEYIA KTPQVRDVLL SGGDALLVSD
KKLESIIQKL RAIPHVEIIR IGSRTPVVLP QRITPELCNM LKKYHPIWLN THFNHPQEVT
PEAKKACEML ADAGVPLGNQ TVLLRGINDS VPVMKRLVHD LVMMRVRPYY IYQCDLSMGL
EHFRTPVSKG IEIIEGLRGH TSGYAVPTFV VDAPGGGGKT PVMPQYVISQ SPHRVVLRNF
EGVITTYTEP ENYTHEPCYD EEKFEKMYEI SGVYMLDEGL KMSLEPSHLA RHERNKKRAE
AEGKK
