NASF_BACSU
ID NASF_BACSU Reviewed; 483 AA.
AC P42437;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Uroporphyrinogen-III C-methyltransferase;
DE Short=Urogen III methylase;
DE EC=2.1.1.107;
DE AltName: Full=SUMT;
DE AltName: Full=Uroporphyrinogen III methylase;
DE Short=UROM;
GN Name=nasF; Synonyms=nasBE; OrderedLocusNames=BSU03280;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7868621; DOI=10.1128/jb.177.5.1409-1413.1995;
RA Ogawa K., Akagawa E., Yamane K., Sun Z.-W., Lacelle M., Zuber P.,
RA Nakano M.M.;
RT "The nasB operon and nasA gene are required for nitrate/nitrite
RT assimilation in Bacillus subtilis.";
RL J. Bacteriol. 177:1409-1413(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION BY TNRA.
RC STRAIN=168;
RX PubMed=10864496; DOI=10.1006/jmbi.2000.3846;
RA Wray L.V. Jr., Zalieckas J.M., Fisher S.H.;
RT "Purification and in vitro activities of the Bacillus subtilis TnrA
RT transcription factor.";
RL J. Mol. Biol. 300:29-40(2000).
RN [5]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) +
CC precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107;
CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC conditions. {ECO:0000269|PubMed:10864496, ECO:0000269|PubMed:12823818}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; D30689; BAA06356.1; -; Genomic_DNA.
DR EMBL; D50453; BAA08962.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12122.1; -; Genomic_DNA.
DR PIR; I40031; I40031.
DR RefSeq; NP_388210.1; NC_000964.3.
DR RefSeq; WP_003234641.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P42437; -.
DR SMR; P42437; -.
DR STRING; 224308.BSU03280; -.
DR PaxDb; P42437; -.
DR PRIDE; P42437; -.
DR EnsemblBacteria; CAB12122; CAB12122; BSU_03280.
DR GeneID; 938324; -.
DR KEGG; bsu:BSU03280; -.
DR PATRIC; fig|224308.43.peg.336; -.
DR eggNOG; COG0007; Bacteria.
DR eggNOG; COG1587; Bacteria.
DR InParanoid; P42437; -.
DR OMA; IAWKERK; -.
DR PhylomeDB; P42437; -.
DR BioCyc; BSUB:BSU03280-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IBA:GO_Central.
DR CDD; cd11642; SUMT; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 1.
DR Gene3D; 3.40.50.10090; -; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR006366; CobA/CysG_C.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR SUPFAM; SSF69618; SSF69618; 1.
DR TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1.
DR PROSITE; PS00839; SUMT_1; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Porphyrin biosynthesis; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..483
FT /note="Uroporphyrinogen-III C-methyltransferase"
FT /id="PRO_0000150384"
SQ SEQUENCE 483 AA; 53869 MW; 49752620FA96B74C CRC64;
MIMKNGIVYF VGAGPGDPGL LTIKGKQALK EADVILYDRL ANPKLLEFAS PDCQFIYCGK
LPNRHFMKQK EINALLVEKA LNGLTVVRLK GGDPSVFGRV GEEADALHEH GIRYEMVPGI
TSGIAAPLYA GIPVTHRDFA SSFAMITAHD KSLKGTPNLD WEGLARSVQT LVFYMGVKNL
SYICQQLISY GKSPSVPVIV IQWGTWGRQR SVKGTLENIQ QKVQEHQITN PAIIVIGDIV
NFQTHSWFES KPLIGRHLMV VTHGEDEDPL ADKLRDSGAD LIEWPKWRTE NMPVNEEILR
KIGTFEDVFF TSRRAVCEFF RALASQKIDI RQLTAKLSAA SEQAKTELEK RGFLVTAIQP
DSEKRLVVGS RHAVENMQKH ESCSFYITHE NVIDDRFTHM IQRTISESPL HMVICPNKLS
VQQLINGGEQ IGILPEPSAS RPPIVCIGDD SAAGIYGFTA VQEQDELLAF IHNQHAEKKL
LHT