KAMD_FUSNN
ID KAMD_FUSNN Reviewed; 518 AA.
AC Q8RHX7;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Lysine 5,6-aminomutase alpha subunit {ECO:0000305};
DE Short=5,6-LAM {ECO:0000305};
DE EC=5.4.3.3 {ECO:0000250|UniProtKB:E3PRJ5, ECO:0000269|PubMed:6811551};
DE AltName: Full=D-lysine 5,6-aminomutase alpha subunit {ECO:0000250|UniProtKB:E3PRJ5};
DE AltName: Full=L-beta-lysine 5,6-aminomutase alpha subunit {ECO:0000312|EMBL:AAL93962.1};
GN OrderedLocusNames=FN1863;
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]
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]
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 migration of the L-beta-lysine and D-lysine
CC epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate
CC and 2,5-diaminohexanoate, respectively. {ECO:0000250|UniProtKB:E3PRJ5,
CC ECO:0000269|PubMed:6811551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate;
CC Xref=Rhea:RHEA:21736, ChEBI:CHEBI:57434, ChEBI:CHEBI:57436;
CC EC=5.4.3.3; Evidence={ECO:0000269|PubMed:6811551};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-lysine = (2R,5S)-2,5-diaminohexanoate; Xref=Rhea:RHEA:18241,
CC ChEBI:CHEBI:32557, ChEBI:CHEBI:137487; EC=5.4.3.3;
CC Evidence={ECO:0000250|UniProtKB:E3PRJ5};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000250|UniProtKB:E3PRJ5};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:E3PRJ5};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via acetate
CC pathway. {ECO:0000269|PubMed:6811551}.
CC -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta subunits.
CC {ECO:0000250|UniProtKB:E3PRJ5}.
CC -!- SIMILARITY: Belongs to the KamD family. {ECO:0000255}.
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DR EMBL; AE009951; AAL93962.1; -; Genomic_DNA.
DR RefSeq; NP_602663.1; NC_003454.1.
DR AlphaFoldDB; Q8RHX7; -.
DR SMR; Q8RHX7; -.
DR STRING; 190304.FN1863; -.
DR PRIDE; Q8RHX7; -.
DR EnsemblBacteria; AAL93962; AAL93962; FN1863.
DR KEGG; fnu:FN1863; -.
DR PATRIC; fig|190304.8.peg.339; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_517447_0_0_0; -.
DR OMA; SGLCMPE; -.
DR BioCyc; FNUC190304:G1FZS-360-MON; -.
DR BioCyc; MetaCyc:MON-13527; -.
DR BRENDA; 5.4.3.3; 2370.
DR UniPathway; UPA00870; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0047702; F:beta-lysine 5,6-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0047826; F:D-lysine 5,6-aminomutase activity; IEA:RHEA.
DR GO; GO:0019475; P:L-lysine catabolic process to acetate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.440; -; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR015130; Lys-AminoMut_A.
DR InterPro; IPR037086; Lys-AminoMut_asu_sf.
DR Pfam; PF09043; Lys-AminoMut_A; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
PE 1: Evidence at protein level;
KW Cobalamin; Cobalt; Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..518
FT /note="Lysine 5,6-aminomutase alpha subunit"
FT /id="PRO_0000416983"
FT BINDING 184..189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ5"
FT BINDING 238
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ5"
FT BINDING 263
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ5"
FT BINDING 268
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ5"
FT BINDING 299
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:E3PRJ5"
SQ SEQUENCE 518 AA; 57323 MW; CC925BC71C5AD436 CRC64;
MGKLDLDWGL VKEARESAKK IAADAQVFID AHSTVTVERT ICRLLGIDGV DEFGVPLPNV
IVDFIKDNGN ISLGVAKYIG NAMIETKLQP QEIAEKVAKK ELDITKMQWH DDFDIQLALK
DITHSTVERI KANRKAREDY LEQFGGDKKG PYIYVIVATG NIYEDVTQAV AAARQGADVV
AVIRTTGQSL LDFVPFGATT EGFGGTMATQ ENFRIMRKAL DDVGVELGRY IRLCNYCSGL
CMPEIAAMGA LERLDMMLND ALYGILFRDI NMKRTLVDQF FSRIINGFAG VIINTGEDNY
LTTADAIEEA HTVLASQFIN EQFALVAGLP EEQMGLGHAF EMEPGTENGF LLELAQAQMA
REIFPKAPLK YMPPTKFMTG NIFKGHIQDA LFNIVTITTG QKVHLLGMLT EAIHTPFMSD
RALSIENARY IFNNLKDFGN DIEFKKGGIM NTRAQEVLKK AAELLKTIET MGIFKTIEKG
VFGGVRRPID GGKGLAGVFE KDNTYFNPFI PLMLGGDR
