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Database: UniProt
Entry: A0A2M9D0B4_9CELL
LinkDB: A0A2M9D0B4_9CELL
Original site: A0A2M9D0B4_9CELL 
ID   A0A2M9D0B4_9CELL        Unreviewed;       409 AA.
AC   A0A2M9D0B4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=uroporphyrinogen-III C-methyltransferase {ECO:0000256|ARBA:ARBA00012162};
DE            EC=2.1.1.107 {ECO:0000256|ARBA:ARBA00012162};
GN   ORFNames=CLV28_0764 {ECO:0000313|EMBL:PJJ77543.1};
OS   Sediminihabitans luteus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Sediminihabitans.
OX   NCBI_TaxID=1138585 {ECO:0000313|EMBL:PJJ77543.1, ECO:0000313|Proteomes:UP000231693};
RN   [1] {ECO:0000313|EMBL:PJJ77543.1, ECO:0000313|Proteomes:UP000231693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25478 {ECO:0000313|EMBL:PJJ77543.1,
RC   ECO:0000313|Proteomes:UP000231693};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJJ77543.1}.
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DR   EMBL; PGFE01000001; PJJ77543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9D0B4; -.
DR   OrthoDB; 9815856at2; -.
DR   Proteomes; UP000231693; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:InterPro.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:InterPro.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA/CysG_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR012409; Sirohaem_synth.
DR   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF13241; NAD_binding_7; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036426; Sirohaem_synth; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:PJJ77543.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231693};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PJJ77543.1}.
FT   DOMAIN          171..383
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ   SEQUENCE   409 AA;  41928 MW;  1FDFAB76F0378FCB CRC64;
     MTTLLGVDVA GRDVLVAGGG PVAARRARAL VADGAHVRVV APWACEDLRD LVATPDAVGP
     GRGTVRWDER EVVEADVDGA WLVHAATDST TVNRDVARWA EARRTWCVVA SEVDDGTART
     PAVTRSGDVV VGVVSAHGAD PRRARGVRDA IAEHLRTGVD QRRRRTGPGS VVLVGGGPGA
     VDLLTVRGRR ALAEADVVVT DRLGPTGVLD ELAPGVEVVD VGKTPGHHAV PQHEINAILV
     EQARRGRRVV RLKGGDPFVF GRGGEEVDAC REAGVAVEVV PGISSALSVP ALAGIPLTHR
     GTVAAFHVVT GHDSAGRATL DAAAVASVVE RAATLVVLMG VSALDAIAAQ LTAAGADAAT
     PVAIVERGST PQQRVTRSTL ADVARRAGEV GVRAPAVIVV GDVAALDLA
//
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