Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for B4EWC2

Entry ID Method Resolution Chain Position Source
AF-B4EWC2-F1 Predicted AlphaFoldDB

No variants for B4EWC2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B4EWC2

No associated diseases with B4EWC2

2 regional properties for B4EWC2

Type Name Position InterPro Accession
domain Cobalamin-independent methionine synthase MetE, C-terminal/archaeal 429 - 751 IPR002629
domain Cobalamin-independent methionine synthase MetE, N-terminal 5 - 313 IPR013215

Functions

Description
EC Number 2.1.1.14 Methyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Catalysis of the reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
methionine biosynthetic process The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
methylation The process in which a methyl group is covalently attached to a molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTIRNHTLGF PRIGLNRELK KAQESYWAGN ISQAELLAVG KELRARHWQQ QANAGVELLP
70 80 90 100 110 120
VGDFAWYDQV LGTSLLLGNI PPRHRNEDGR LDLDTLFRVA RGRAPTGKPA AASEMTKWFN
130 140 150 160 170 180
TNYHYIVPEF QQGQSFTLAW QQLLDEVDEA LALGHNVKPV LLGPITYLWL GKVKGPEFDR
190 200 210 220 230 240
LSLLDAILPV YQQVLSQLQQ KGIEWVQIDE PALVLDLPIE WQNAYQVAYQ ALTGQVKLLL
250 260 270 280 290 300
TTYFDGITHH LDIIKNLPVN GLHIDLCAGQ DALQVIHQAL PKDWVLSLGV INGRNVWKAD
310 320 330 340 350 360
LTTRYQQVVA LKGKRPLWIG TSCSLLHSPI DLSAETKLDD EVKSWFAFAV QKCAEVALLA
370 380 390 400 410 420
KALNAPEGEY DEQLAQYSAP IRQREHSSRV HNAKVAARLQ AINAQDGERT SPYQQRAKVQ
430 440 450 460 470 480
RARFNFPLWP TTTIGSFPQT TEIRTVRLDF KKGRIDTTAY RTNISEHIKQ AIDEQERLGL
490 500 510 520 530 540
DVLVHGEAER NDMVEYFGEH FEGYVFTQNG WVQSYGSRCV KPPVIIGDIS RPAPITVDWA
550 560 570 580 590 600
TYAQSLTDKP VKGMLTGPVT ILCWSFPRED VSRETIAKQI ALALRDEVDD LQKAGIGIIQ
610 620 630 640 650 660
IDEPALREGL PLRRDEWQAY LDWAVDAFKL SAAIADDETQ IHTHMCYCEF NDIMEAIAAL
670 680 690 700 710 720
DADVITIETS RSDMELLEAF EHFDYPNEIG PGVYDIHSPN VPNVEWIVGL LRKAQSRIPA
730 740 750
ERLWVNPDCG LKTRGWSETR AALANMVEAA KYLRQNV