ID MAAL_CLOTT Reviewed; 413 AA. AC Q05514; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 20-JAN-2009, entry version 55. DE RecName: Full=Methylaspartate ammonia-lyase; DE EC=4.3.1.2; DE AltName: Full=Beta-methylaspartase; OS Clostridium tetanomorphum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1553; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-26. RC STRAIN=ATCC 15920 / DSM 528 / H1; RX MEDLINE=93041773; PubMed=1420191; DOI=10.1021/bi00159a015; RA Goda S.K., Minton N.P., Botting N.P., Gani D.; RT "Cloning, sequencing, and expression in Escherichia coli of the RT Clostridium tetanomorphum gene encoding beta-methylaspartase and RT characterization of the recombinant protein."; RL Biochemistry 31:10747-10756(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24, AND PROTEIN SEQUENCE OF RP 1-24. RC STRAIN=ATCC 15920 / DSM 528 / H1; RX MEDLINE=93202282; PubMed=8454064; DOI=10.1016/0014-5793(93)80042-S; RA Brecht M., Kellermann J., Plueckthun A.; RT "Cloning and sequencing of glutamate mutase component E from RT Clostridium tetanomorphum."; RL FEBS Lett. 319:84-89(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71. RC STRAIN=NCIMB 11547; RX MEDLINE=93154518; PubMed=8428631; DOI=10.1016/0014-5793(93)81488-L; RA Holloway D.E., Marsh E.N.G.; RT "Cloning and sequencing of glutamate mutase component E from RT Clostridium tetanomorphum. Organization of the mut genes."; RL FEBS Lett. 317:44-48(1993). RN [4] RP PROTEIN SEQUENCE OF 1-15. RC STRAIN=NCIMB 11547; RX MEDLINE=93011908; PubMed=1397267; DOI=10.1016/0014-5793(92)81321-C; RA Marsh E.N.G., Holloway D.E.; RT "Cloning and sequencing of glutamate mutase component S from RT Clostridium tetanomorphum. Homologies with other cobalamin-dependent RT enzymes."; RL FEBS Lett. 310:167-170(1992). CC -!- CATALYTIC ACTIVITY: L-threo-3-methylaspartate = mesaconate + CC NH(3). CC -!- COFACTOR: Cobalamin. CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via CC mesaconate pathway; acetate and pyruvate from L-glutamate: step CC 2/4. CC -!- SUBUNIT: Homodimer. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S48141; AAB24070.1; -; Genomic_DNA. DR EMBL; X70499; CAA49911.1; -; Genomic_DNA. DR EMBL; X70695; CAA50027.1; -; Genomic_DNA. DR PIR; B44285; B44285. DR PDB; 1KCZ; X-ray; 1.90 A; A/B=1-413. DR PDB; 1KD0; X-ray; 1.90 A; A/B=1-413. DR PDBsum; 1KCZ; -. DR PDBsum; 1KD0; -. DR BioCyc; MetaCyc:MON-1103; -. DR BRENDA; 4.3.1.2; 2080. DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW. DR GO; GO:0050096; F:methylaspartate ammonia-lyase activity; IEA:EC. DR InterPro; IPR006395; Met_Asp_am_lyase. DR Pfam; PF07476; MAAL_C; 1. DR Pfam; PF05034; MAAL_N; 1. DR PIRSF; PIRSF017107; MAL; 1. DR TIGRFAMs; TIGR01502; B_methylAsp_ase; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Lyase. FT CHAIN 1 413 Methylaspartate ammonia-lyase. FT /FTId=PRO_0000084547. FT STRAND 2 11 FT STRAND 14 18 FT HELIX 20 24 FT STRAND 28 30 FT STRAND 33 36 FT STRAND 44 49 FT STRAND 52 59 FT STRAND 64 69 FT TURN 73 76 FT HELIX 86 96 FT HELIX 98 101 FT HELIX 109 118 FT HELIX 128 146 FT HELIX 150 158 FT HELIX 179 186 FT STRAND 190 194 FT HELIX 200 204 FT HELIX 209 225 FT STRAND 234 238 FT HELIX 242 246 FT TURN 247 249 FT HELIX 251 265 FT STRAND 270 273 FT HELIX 281 298 FT STRAND 302 306 FT HELIX 313 321 FT STRAND 325 330 FT HELIX 333 335 FT HELIX 339 350 FT STRAND 354 357 FT HELIX 365 378 FT STRAND 381 384 FT STRAND 387 391 FT HELIX 392 410 SQ SEQUENCE 413 AA; 45534 MW; 4451923DB035EF13 CRC64; MKIVDVLCTP GLTGFYFDDQ RAIKKGAGHD GFTYTGSTVT EGFTQVRQKG ESISVLLVLE DGQVAHGDCA AVQYSGAGGR DPLFLAKDFI PVIEKEIAPK LIGREITNFK PMAEEFDKMT VNGNRLHTAI RYGITQAILD AVAKTRKVTM AEVIRDEYNP GAEINAVPVF AQSGDDRYDN VDKMIIKEAD VLPHALINNV EEKLGLKGEK LLEYVKWLRD RIIKLRVRED YAPIFHIDVY GTIGAAFDVD IKAMADYIQT LAEAAKPFHL RIEGPMDVED RQKQMEAMRD LRAELDGRGV DAELVADEWC NTVEDVKFFT DNKAGHMVQI KTPDLGGVNN IADAIMYCKA NGMGAYCGGT CNETNRSAEV TTNIGMACGA RQVLAKPGMG VDEGMMIVKN EMNRVLALVG RRK //