OAMS_ACESD
ID OAMS_ACESD Reviewed; 121 AA.
AC E3PY96; Q8VPJ6;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=D-ornithine 4,5-aminomutase subunit alpha;
DE EC=5.4.3.5 {ECO:0000312|EMBL:CBH21411.1};
DE AltName: Full=D-ornithine aminomutase S component {ECO:0000303|PubMed:11577113};
DE Short=OAM-S;
GN Name=oraS; OrderedLocusNames=CLOST_1291;
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] {ECO:0000305, ECO:0000312|EMBL:AAK72501.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000269|PubMed:11577113};
RX PubMed=11577113; DOI=10.1074/jbc.m108365200;
RA Chen H.P., Wu S.H., Lin Y.L., Chen C.M., Tsay S.S.;
RT "Cloning, sequencing, heterologous expression, purification, and
RT characterization of adenosylcobalamin-dependent D-ornithine aminomutase
RT from Clostridium sticklandii.";
RL J. Biol. Chem. 276:44744-44750(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
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).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000269|PubMed:4711468};
RX PubMed=4711468; DOI=10.1021/bi00738a008;
RA Somack R., Costilow R.N.;
RT "Purification and properties of a pyridoxal phosphate and coenzyme B 12
RT dependent D-ornithine 5,4-aminomutase.";
RL Biochemistry 12:2597-2604(1973).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RA Baker J.J., Stadtman T.C.;
RT "Amino mutases.";
RL (In) Dolphin D. (eds.);
RL B12, pp.2:203-231, Wiley Interscience, New York (1982).
RN [5] {ECO:0000305, ECO:0000312|PDB:3KP0}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH ORAE SUBUNIT, AND
RP SUBUNIT.
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000269|PubMed:20106986};
RX PubMed=20106986; DOI=10.1074/jbc.m109.068908;
RA Wolthers K.R., Levy C., Scrutton N.S., Leys D.;
RT "Large-scale domain dynamics and adenosylcobalamin reorientation
RT orchestrate radical catalysis in ornithine 4,5-aminomutase.";
RL J. Biol. Chem. 285:13942-13950(2010).
CC -!- FUNCTION: Component of a complex that catalyzes the reversible
CC migration of the omega amino group of D-ornithine to C-4 to form
CC (2R,4S)-2,4-diaminopentanoic acid. The role of OraS remains obscure;
CC however, it seems to be required for a correct folding of the OraE
CC subunit. The complex is active only on D-ornithine and 2,4-
CC diaminopentanoic acid and not active on L-ornithine, L-beta-lysine, L-
CC alpha-lysine or D-alpha-lysine. {ECO:0000269|PubMed:11577113,
CC ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ornithine = (2R,4S)-2,4-diaminopentanoate;
CC Xref=Rhea:RHEA:14893, ChEBI:CHEBI:57668, ChEBI:CHEBI:58697;
CC EC=5.4.3.5; Evidence={ECO:0000269|PubMed:11577113,
CC ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4};
CC -!- ACTIVITY REGULATION: Increased activity in the presence of
CC dithiothreitol (DTT) in vitro. Inhibited by 1 mM potassium phosphate
CC and potassium chloride. Inhibited by L-alpha-ornithine, D,L-alpha-
CC lysine, L-beta-lysine (50%-60%), L-alpha-lysine (26%) and by delta-
CC amino-n-valeric acid to a lesser extent. Significant decrease in
CC activity is observed in the presence of 0.2 mM p-chloromercuribenzoate,
CC N-ethylmaleimide and also by 2 mM iodoacetate to a lesser extent but
CC not inhibited by arsenite. {ECO:0000269|PubMed:4711468,
CC ECO:0000269|Ref.4}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0 or between 8.5-8.7 (with Tris-HCl buffer). Half-
CC maximal activity is observed at pH 7.4 and 9.7.
CC {ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for native enzyme. Displays
CC half-maximal activity at 23 degrees Celsius and 49 degrees Celsius.
CC Rapidly inactivated at temperatures above 45 degrees Celsius. Loses
CC more than 35% and 30% of its activity when stored at -20 degrees
CC Celsius for 1 month and at 4 degrees Celsius for 48 hours,
CC respectively. {ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4};
CC -!- SUBUNIT: Heterotetramer of 2 alpha (OraS) and 2 beta (OraE) subunits.
CC {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:20106986,
CC ECO:0000269|Ref.4}.
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; AY038595; AAK72501.1; -; Genomic_DNA.
DR EMBL; FP565809; CBH21411.1; -; Genomic_DNA.
DR PDB; 3KOW; X-ray; 2.90 A; E/F/G/H=1-121.
DR PDB; 3KOX; X-ray; 2.40 A; E/F/G/H=1-121.
DR PDB; 3KOY; X-ray; 2.80 A; E/F/G/H=1-121.
DR PDB; 3KOZ; X-ray; 2.80 A; E/F/G/H=1-121.
DR PDB; 3KP0; X-ray; 2.80 A; E/F/G/H=1-121.
DR PDB; 3KP1; X-ray; 2.01 A; E/F/G/H=1-121.
DR PDBsum; 3KOW; -.
DR PDBsum; 3KOX; -.
DR PDBsum; 3KOY; -.
DR PDBsum; 3KOZ; -.
DR PDBsum; 3KP0; -.
DR PDBsum; 3KP1; -.
DR AlphaFoldDB; E3PY96; -.
DR SMR; E3PY96; -.
DR STRING; 1511.CLOST_1291; -.
DR EnsemblBacteria; CBH21411; CBH21411; CLOST_1291.
DR KEGG; cst:CLOST_1291; -.
DR eggNOG; ENOG5032S0N; Bacteria.
DR HOGENOM; CLU_153213_0_0_9; -.
DR OMA; GAGHIVW; -.
DR BioCyc; MetaCyc:MON-12492; -.
DR BRENDA; 5.4.3.5; 1522.
DR EvolutionaryTrace; E3PY96; -.
DR Proteomes; UP000007041; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0047831; F:D-ornithine 4,5-aminomutase activity; IEA:UniProtKB-EC.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR015130; Lys-AminoMut_A.
DR Pfam; PF16552; OAM_alpha; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Reference proteome.
FT CHAIN 1..121
FT /note="D-ornithine 4,5-aminomutase subunit alpha"
FT /id="PRO_0000421804"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 19..43
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:3KP1"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:3KP1"
SQ SEQUENCE 121 AA; 13623 MW; 62D4FC5EA0087F86 CRC64;
MKRADDFQQR RAHLANLSDE ELQTRFWEMA EKIVDPLLDL GKKNTTPSIE RSVLLRMGFS
SLEAKAIVDK TMDRGLMGKG AGHIVYKIAK EKNISVREAG LALSEGKYWD DAIQIFKGGV
K
