HEM3_BACSU
ID HEM3_BACSU Reviewed; 314 AA.
AC P16616;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Porphobilinogen deaminase;
DE Short=PBG;
DE EC=2.5.1.61;
DE AltName: Full=Hydroxymethylbilane synthase;
DE Short=HMBS;
DE AltName: Full=Pre-uroporphyrinogen synthase;
GN Name=hemC; OrderedLocusNames=BSU28150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2110138; DOI=10.1128/jb.172.5.2250-2258.1990;
RA Petricek M., Rutberg L., Schroeder I., Hederstedt L.;
RT "Cloning and characterization of the hemA region of the Bacillus subtilis
RT chromosome.";
RL J. Bacteriol. 172:2250-2258(1990).
RN [2]
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).
CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+);
CC Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Note=Binds 1 dipyrromethane group covalently.;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC -!- SUBUNIT: Monomer.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethane group. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}.
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DR EMBL; M57676; AAA22512.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14775.1; -; Genomic_DNA.
DR PIR; C35252; IBBS.
DR RefSeq; NP_390693.1; NC_000964.3.
DR RefSeq; WP_010886587.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P16616; -.
DR SMR; P16616; -.
DR STRING; 224308.BSU28150; -.
DR jPOST; P16616; -.
DR PaxDb; P16616; -.
DR PRIDE; P16616; -.
DR EnsemblBacteria; CAB14775; CAB14775; BSU_28150.
DR GeneID; 937488; -.
DR KEGG; bsu:BSU28150; -.
DR PATRIC; fig|224308.43.peg.2942; -.
DR eggNOG; COG0181; Bacteria.
DR InParanoid; P16616; -.
DR OMA; LWQANHI; -.
DR PhylomeDB; P16616; -.
DR BioCyc; BSUB:BSU28150-MON; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.160.40; -; 1.
DR HAMAP; MF_00260; Porphobil_deam; 1.
DR InterPro; IPR000860; HemC.
DR InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR InterPro; IPR022417; Porphobilin_deaminase_N.
DR InterPro; IPR022418; Porphobilinogen_deaminase_C.
DR InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR PANTHER; PTHR11557; PTHR11557; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR Pfam; PF03900; Porphobil_deamC; 1.
DR PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF54782; SSF54782; 1.
DR TIGRFAMs; TIGR00212; hemC; 1.
DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE 3: Inferred from homology;
KW Porphyrin biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..313
FT /note="Porphobilinogen deaminase"
FT /id="PRO_0000142910"
FT MOD_RES 242
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 34838 MW; A4F13170243E874D CRC64;
MMRTIKVGSR RSKLAMTQTK WVIQKLKEIN PSFAFEIKEI VTKGDRIVDV TLSKVGGKGL
FVKEIEQALL NEEIDMAVHS MKDMPAVLPE GLVIGCIPER EDPRDALISK NRVKLSEMKK
GAVIGTSSLR RSAQLLIERP DLTIKWIRGN IDTRLQKLET EDYDAIILAA AGLSRMGWKQ
DVVTEFLEPE RCLPAVGQGA LAIECRESDE ELLALFSQFT DEYTKRTVLA ERAFLNAMEG
GCQVPIAGYS VLNGQDEIEM TGLVASPDGK IIFKETVTGN DPEEVGKRCA ALMADKGAKD
LIDRVKRELD EDGK